Abstract
Biological or therapeutic targeting could be defined as the mechanism(s) by which a biological cargo (drug) is transported to its proper destination, in case of a patient to specific parts of the body, such as diseased tissue.
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References
Abbott, N. J., Ronnback, L., & Hansson, E. (2006). Astrocyte-endothelial interactions at the blood-brain barrier. Nature Reviews Neuroscience, 7, 41–53.
Acar, H., Ting, J. M., Srivastava, S., Labelle, J. L., & Tirrell, M. V. (2017). Molecular engineering solutions for therapeutic peptide delivery. Chem Soc Rev.
Alexander-Bryant, A. A., Dumitriu, A., Attaway, C. C., Yu, H., & Jakymiw, A. (2015). Fusogenic-oligoarginine peptide-mediated silencing of the CIP2A oncogene suppresses oral cancer tumor growth in vivo. Journal of Control Release, 218, 72–81.
Alexander-Bryant, A. A., Zhang, H., Attaway, C. C., Pugh, W., Eggart, L., Sansevere, R. M., et al. (2017). Dual peptide-mediated targeted delivery of bioactive siRNAs to oral cancer cells in vivo. Oral Oncology, 72, 123–131.
Alhakamy, N. A., Ishiguro, S., Uppalapati, D., Berkland, C. J., & Tamura, M. (2016). AT2R gene delivered by condensed polylysine complexes attenuates Lewis lung carcinoma after intravenous injection or intratracheal spray. Molecular Cancer Therapeutics, 15, 209–218.
Ali, N., Mattsson, K., Rissler, J., Karlsson, H. M., Svensson, C. R., Gudmundsson, A., et al. (2016). Analysis of nanoparticle-protein coronas formed in vitro between nanosized welding particles and nasal lavage proteins. Nanotoxicology, 10, 226–234.
Almansour, K., Taverner, A., Turner, J. R., Eggleston, I. M., & Mrsny, R. J. (2018). An intestinal paracellular pathway biased toward positively-charged macromolecules. Journal of Control Release.
Alta, R. Y. P., Vitorino, H. A., Goswami, D., Liria, C. W., Wisnovsky, S. P., Kelley, S. O., et al. (2017). Mitochondria-penetrating peptides conjugated to desferrioxamine as chelators for mitochondrial labile iron. PLoS ONE, 12, e0171729.
Althuon, D., Ronicke, F., Furniss, D., Quan, J., Wellhofer, I., Jung, N., et al. (2015). Functionalized triazolopeptoids—a novel class for mitochondrial targeted delivery. Organic and Biomolecular Chemistry, 13, 4226–4230.
Anchordoquy, T. J., Barenholz, Y., Boraschi, D., Chorny, M., Decuzzi, P., Dobrovolskaia, M. A., et al. (2017). Mechanisms and barriers in cancer nanomedicine: Addressing challenges, looking for solutions. ACS Nano, 11, 12–18.
Appelqvist, H., Waster, P., Kagedal, K., & Ollinger, K. (2013). The lysosome: From waste bag to potential therapeutic target. Journal of Molecular Cell Biology, 5, 214–226.
Apte, A., Koren, E., Koshkaryev, A., & Torchilin, V. P. (2014). Doxorubicin in TAT peptide-modified multifunctional immunoliposomes demonstrates increased activity against both drug-sensitive and drug-resistant ovarian cancer models. Cancer Biology and Therapy, 15, 69–80.
Araujo, F., Shrestha, N., Shahbazi, M. A., Liu, D., Herranz-Blanco, B., Makila, E. M., et al. (2015). Microfluidic assembly of a multifunctional tailorable composite system designed for site specific combined oral delivery of peptide drugs. ACS Nano, 9, 8291–8302.
Aronov, O., Horowitz, A. T., Gabizon, A., Fuertes, M. A., Perez, J. M., & Gibson, D. (2004). Nuclear localization signal-targeted poly(ethylene glycol) conjugates as potential carriers and nuclear localizing agents for carboplatin analogues. Bioconjugate Chemistry, 15, 814–823.
Arosio, D., & Casagrande, C. (2016). Advancement in integrin facilitated drug delivery. Advanced Drug Delivery Reviews, 97, 111–143.
Arroyo, J. D., Jourdain, A. A., Calvo, S. E., Ballarano, C. A., Doench, J. G., Root, D. E., et al. (2016). A genome-wide CRISPR death screen identifies genes essential for oxidative phosphorylation. Cell Metabolism, 24, 875–885.
Bae, H. D., Lee, J., Jin, X. H., & Lee, K. (2016). Potential of translationally controlled tumor protein-derived protein transduction domains as antigen carriers for nasal vaccine delivery. Molecular Pharmaceutics, 13, 3196–3205.
Bae, H. D., Lee, J., Jun, K. Y., Kwon, Y., & Lee, K. (2018). Modification of translationally controlled tumor protein-derived protein transduction domain for improved intranasal delivery of insulin. Drug Delivery, 25, 1025–1032.
Baker, R. D., Howl, J., & Nicholl, I. D. (2007). A sychnological cell penetrating peptide mimic of p21(WAF1/CIP1) is pro-apoptogenic. Peptides, 28, 731–740.
Banks, W. A. (2015). Peptides and the blood-brain barrier. Peptides, 72, 16–19.
Banks, W. A., Kastin, A. J., Huang, W., Jaspan, J. B., & Maness, L. M. (1996). Leptin enters the brain by a saturable system independent of insulin. Peptides, 17, 305–311.
Barbari, G. R., Dorkoosh, F., Amini, M., Bahari Javan, N., Sharifzadeh, M., Atyabi, F., et al. (2018). Synthesis and characterization of a novel peptide-grafted Cs and evaluation of its nanoparticles for the oral delivery of insulin, in vitro, and in vivo study. International Journal of Nanomedicine, 13, 5127–5138.
Barnes, W. J., & Anderson, C. T. (2017). Release, recycle, rebuild: Cell wall remodeling, autodegradation, and sugar salvage for new wall biosynthesis during plant development. Molecular Plant.
Batista da Cunha, D., Pupo Silvestrini, A. V., Gomes da Silva, A. C., Maria de Paula Estevam, D., Pollettini, F. L., De Oliveira Navarro, J., et al. (2018). Mechanistic insights into functional characteristics of native crotamine. Toxicon, 146, 1–12.
Begley, D. J., & Brightman, M. W. (2003). Structural and functional aspects of the blood-brain barrier. Progress in Drug Research, 61, 39–78.
Ben Djemaa, S., David, S., Herve-Aubert, K., Falanga, A., Galdiero, S., Allard-Vannier, E., et al. (2018). Formulation and in vitro evaluation of a siRNA delivery nanosystem decorated with gH625 peptide for triple negative breast cancer theranosis. European Journal of Pharmaceutics and Biopharmaceutics.
Berry, C. C., de la Fuente, J. M., Mullin, M., Chu, S. W., & Curtis, A. S. (2007). Nuclear localization of HIV-1 tat functionalized gold nanoparticles. IEEE Transactions on Nanobioscience, 6, 262–269.
Bertrand, N., & Leroux, J.-C. (2012). The journey of a drug-carrier in the body: An anatomo-physiological perspective. Journal of Controlled Release, 161, 152–163.
Bhunia, D., Mondal, P., Das, G., Saha, A., Sengupta, P., Jana, J., et al. (2018). Spatial position regulates power of tryptophan: Discovery of a major-groove-specific nuclear-localizing, cell-penetrating tetrapeptide. Journal of the American Chemical Society.
Bhutia, S. K., Mallick, S. K., Maiti, S., Mishra, D., & Maiti, T. K. (2009). Abrus abrin derived peptides induce apoptosis by targeting mitochondria in HeLa cells. Cell Biology International, 33, 720–727.
Bidwell, G. L., III, Davis, A. N., & Raucher, D. (2009). Targeting a c-Myc inhibitory polypeptide to specific intracellular compartments using cell penetrating peptides. Journal of Controlled Release, 135, 2–10.
Bilichak, A., Luu, J., & Eudes, F. (2015). Intracellular delivery of fluorescent protein into viable wheat microspores using cationic peptides. Frontiers in Plant Science, 6.
Biswas, S., Deshpande, P. P., Perche, F., Dodwadkar, N. S., Sane, S. D., & Torchilin, V. P. (2013). Octa-arginine-modified pegylated liposomal doxorubicin: An effective treatment strategy for non-small cell lung cancer. Cancer Letters, 335, 191–200.
Bolhassani, A. (2011). Potential efficacy of cell-penetrating peptides for nucleic acid and drug delivery in cancer. Biochimica et Biophysica Acta, 1816, 232–246.
Bolhassani, A., Jafarzade, B. S., & Mardani, G. (2017). In vitro and in vivo delivery of therapeutic proteins using cell penetrating peptides. Peptides, 87, 50–63.
Bonifacino, J. S., & Dell’Angelica, E. C. (1999). Molecular bases for the recognition of tyrosine-based sorting signals. Journal of Cell Biology, 145, 923–926.
Bowerman, C. J., & Nilsson, B. L. (2010). A reductive trigger for peptide self-assembly and hydrogelation. Journal of the American Chemical Society, 132, 9526–9527.
Brasnjevic, I., Steinbusch, H. W., Schmitz, C., & Martinez-Martinez, P. (2009). Delivery of peptide and protein drugs over the blood-brain barrier. Progress in Neurobiology, 87, 212–251.
Brayden, D. J., & Mrsny, R. J. (2011). Oral peptide delivery: Prioritizing the leading technologies. Therapeutic Delivery, 2, 1567–1573.
Brunner, J., & Barton, J. K. (2006). Targeting DNA mismatches with rhodium intercalators functionalized with a cell-penetrating peptide. Biochemistry, 45, 12295–12302.
Buckley, S. T., Hubalek, F., & Rahbek, U. L. (2016). Chemically modified peptides and proteins—Critical considerations for oral delivery. Tissue Barriers, 4, Apr–Jun.
Cantini, L., Attaway, C. C., Butler, B., Andino, L. M., Sokolosky, M. L., & Jakymiw, A. (2013). Fusogenic-oligoarginine peptide-mediated delivery of siRNAs targeting the CIP2A oncogene into oral cancer cells. PLoS ONE, 8, e73348.
Cardo, L., Thomas, S. G., Mazharian, A., Pikramenou, Z., Rappoport, J. Z., Hannon, M. J., et al. (2015). Accessible synthetic probes for staining actin inside platelets and megakaryocytes by employing lifeact peptide. ChemBioChem, 16, 1680–1688.
Carmichael, N. M., Dostrovsky, J. O., & Charlton, M. P. (2010). Peptide-mediated transdermal delivery of botulinum neurotoxin type A reduces neurogenic inflammation in the skin. Pain, 149, 316–324.
Cerrato, C. P., Künnapuu, K., & Langel, Ü. (2017). Cell-penetrating peptides with intracellular organelle targeting. Expert Opinion on Drug Delivery, 14, 245–255.
Cerrato, C. P., & Langel, U. (2017). Effect of a fusion peptide by covalent conjugation of a mitochondrial cell-penetrating peptide and a glutathione analog peptide. Molecular Therapy-Methods and Clinical Development, 5, 221–231.
Cerrato, C. P., Pirisinu, M., Vlachos, E. N., & Langel, Ü. (2015). Novel cell-penetrating peptide targeting mitochondria. FASEB Journal, 29, 4589–4599.
Chang, M., Chou, J.-C., & Lee, H.-J. (2005). Cellular internalization of fluorescent proteins via arginine-rich intracellular delivery peptide in plant cells. Plant and Cell Physiology, 46, 482–488.
Chang, M., Chou, J. C., Chen, C. P., Liu, B. R., & Lee, H. J. (2007). Noncovalent protein transduction in plant cells by macropinocytosis. New Phytologist, 174, 46–56.
Chen, B., Friedman, B., Whitney, M. A., Winkle, J. A., Lei, I. F., Olson, E. S., et al. (2012). Thrombin activity associated with neuronal damage during acute focal ischemia. Journal of Neuroscience, 32, 7622–7631.
Chen, C.-P., Chou, J.-C., Liu, B. R., Chang, M., & Lee, H.-J. (2007). Transfection and expression of plasmid DNA in plant cells by an arginine-rich intracellular delivery peptide without protoplast preparation. FEBS Letters, 581, 1891–1897.
Chen, H. C., Chiou, S. T., Zheng, J. Y., Yang, S. H., Lai, S. S., & Kuo, T. Y. (2011). The nuclear localization signal sequence of porcine circovirus type 2 ORF2 enhances intracellular delivery of plasmid DNA. Archives of Virology, 156, 803–815.
Chen, M., Kumar, S., Anselmo, A. C., Gupta, V., Slee, D. H., Muraski, J. A., et al. (2015). Topical delivery of Cyclosporine A into the skin using SPACE-peptide. Journal of Control Release, 199, 190–197.
Chen, M., Zakrewsky, M., Gupta, V., Anselmo, A. C., Slee, D. H., Muraski, J. A., et al. (2014a). Topical delivery of siRNA into skin using SPACE-peptide carriers. Journal of Control Release, 179, 33–41.
Chen, Q., & Lai, H. (2015). Gene delivery into plant cells for recombinant protein production. BioMed Research International, 2015, 932161.
Chen, Q., Lai, H., Hurtado, J., Stahnke, J., Leuzinger, K., & Dent, M. (2013). Agroinfiltration as an effective and scalable strategy of gene delivery for production of pharmaceutical proteins. Advanced Techniques in Biology & Medicine, 1.
Chen, Y., & Liu, L. (2012). Modern methods for delivery of drugs across the blood-brain barrier. Advanced Drug Delivery Reviews, 64, 640–665.
Chen, Y., Shen, Y., Guo, X., Zhang, C., Yang, W., Ma, M., et al. (2006). Transdermal protein delivery by a coadministered peptide identified via phage display. Nature Biotechnology, 24, 455–460.
Chen, Z., Zhang, P., Cheetham, A. G., Moon, J. H., Moxley, J. W., Jr., Lin, Y. A. et al. (2014b). Controlled release of free doxorubicin from peptide-drug conjugates by drug loading. Journal of Control Release, 191, 123–130.
Cheng, H., Zhu, J. Y., Xu, X. D., Qiu, W. X., Lei, Q., Han, K., et al. (2015). Activable cell-penetrating peptide conjugated prodrug for tumor targeted drug delivery. ACS Applied Materials and Interfaces, 7, 16061–16069.
Cheng, Y., Huang, F., Min, X., Gao, P., Zhang, T., Li, X., et al. (2016). Protease-responsive prodrug with aggregation-induced emission probe for controlled drug delivery and drug release tracking in living cells. Analytical Chemistry, 88, 8913–8919.
Choi, D. K., Bae, J., Shin, S. M., Shin, J. Y., Kim, S., & Kim, Y. S. (2014). A general strategy for generating intact, full-length IgG antibodies that penetrate into the cytosol of living cells. MAbs, 6, 1402–1414.
Choi, S. W., Pangeni, R., Jung, D. H., Kim, S. J., & Park, J. W. (2018). Construction and characterization of cell-penetrating peptide-fused fibroblast growth factor and vascular endothelial growth factor for an enhanced percutaneous delivery system. Journal of Nanoscience and Nanotechnology, 18, 842–847.
Choi, Y., Kim, K., Hong, S., Kim, H., Kwon, Y. J., & Song, R. (2011). Intracellular protein target detection by quantum dots optimized for live cell imaging. Bioconjugate Chemistry, 22, 1576–1586.
Chuah, J. A., Horii, Y., & Numata, K. (2016a). Peptide-derived method to transport genes and proteins across cellular and organellar barriers in plants. Journal of Visualized Experiments.
Chuah, J. A., Matsugami, A., Hayashi, F., & Numata, K. (2016b). Self-assembled peptide-based system for mitochondrial-targeted gene delivery: Functional and structural insights. Biomacromolecules, 17, 3547–3557.
Chuah, J. A., & Numata, K. (2018). Stimulus-responsive peptide for effective delivery and release of DNA in plants. Biomacromolecules.
Chuah, J. A., Yoshizumi, T., Kodama, Y., & Numata, K. (2015). Gene introduction into the mitochondria of Arabidopsis thaliana via peptide-based carriers. Scientific Reports, 5, 7751.
Chuard, N., Fujisawa, K., Morelli, P., Saarbach, J., Winssinger, N., Metrangolo, P., et al. (2016). Activation of cell-penetrating peptides with Ionpair-pi interactions and fluorophiles. Journal of the American Chemical Society, 138, 11264–11271.
Chugh, A., Amundsen, E., & Eudes, F. (2009). Translocation of cell-penetrating peptides and delivery of their cargoes in triticale microspores. Plant Cell Reports, 28, 801–810.
Chugh, A., & Eudes, F. (2007). Translocation and nuclear accumulation of monomer and dimer of HIV-1 Tat basic domain in triticale mesophyll protoplasts. Biochimica et Biophysica Acta, 1768, 419–426.
Chugh, A., & Eudes, F. (2008a). Cellular uptake of cell-penetrating peptides pVEC and transportan in plants. Journal of Peptide Science, 14, 477–481.
Chugh, A., & Eudes, F. (2008b). Study of uptake of cell penetrating peptides and their cargoes in permeabilized wheat immature embryos. FEBS Journal, 275, 2403–2414.
Cohen-Avrahami, M., Shames, A. I., Ottaviani, M. F., Aserin, A., & Garti, N. (2014). HIV-TAT enhances the transdermal delivery of NSAID drugs from liquid crystalline mesophases. The Journal of Physical Chemistry B, 118, 6277–6287.
Collard, R., Majtan, T., Park, I., & Kraus, J. P. (2018). Import of TAT-conjugated propionyl-CoA carboxylase using models of propionic acidemia. Molecular and Cellular Biology.
Collombet, J.-M., Wheeler, V. C., Vogel, F., & Coutelle, C. (1997). Introduction of plasmid DNA into isolated mitochondria by electroporation: A novel approach toward gene correction for mitochondrial disorders. Journal of Biological Chemistry, 272, 5342–5347.
Colombo, M., Mizzotti, C., Masiero, S., Kater, M. M., & Pesaresi, P. (2015). Peptide aptamers: The versatile role of specific protein function inhibitors in plant biotechnology. Journal of Integrative Plant Biology, 57, 892–901.
Craven, L., Alston, C. L., Taylor, R. W., & Turnbull, D. M. (2017). Recent advances in mitochondrial disease. Annual Review of Genomics and Human Genetics, 17, 091416-035426.
Crisp, J. L., Savariar, E. N., Glasgow, H. L., Ellies, L. G., Whitney, M. A., & Tsien, R. Y. (2014). Dual targeting of integrin alphavbeta3 and matrix metalloproteinase-2 for optical imaging of tumors and chemotherapeutic delivery. Molecular Cancer Therapeutics, 13, 1514–1525.
Danielsen, E. M., & Hansen, G. H. (2018). Impact of cell-penetrating peptides (CPPs) melittin and Hiv-1 Tat on the enterocyte brush border using a mucosal explant system. Biochimica et Biophysica Acta, 1860, 1589–1599.
de Boer, A. G., & Gaillard, P. J. (2007). Strategies to improve drug delivery across the blood-brain barrier. Clinical Pharmacokinetics, 46, 553–576.
de Boer, A. G., van der Sandt, I. C., & Gaillard, P. J. (2003). The role of drug transporters at the blood-brain barrier. Annual Review of Pharmacology and Toxicology, 43, 629–656.
de Kruijf, W., & Ehrhardt, C. (2017). Inhalation delivery of complex drugs-the next steps. Current Opinion in Pharmacology, 36, 52–57.
Deb, R., & Nagotu, S. (2017). Versatility of peroxisomes: An evolving concept. Tissue and Cell, 49, 209–226.
Dekiwadia, C. D., Lawrie, A. C., & Fecondo, J. V. (2012). Peptide-mediated cell penetration and targeted delivery of gold nanoparticles into lysosomes. Journal of Peptide Science, 18, 527–534.
Demeule, M., Poirier, J., Jodoin, J., Bertrand, Y., Desrosiers, R. R., Dagenais, C., et al. (2002). High transcytosis of melanotransferrin (P97) across the blood-brain barrier. Journal of Neurochemistry, 83, 924–933.
Demeule, M., Regina, A., Che, C., Poirier, J., Nguyen, T., Gabathuler, R., et al. (2008). Identification and design of peptides as a new drug delivery system for the brain. Journal of Pharmacology and Experimental Therapeutics, 324, 1064–1072.
Desai, P. R., Cormier, A. R., Shah, P. P., Patlolla, R. R., Paravastu, A. K., & Singh, M. (2014). (31)P solid-state NMR based monitoring of permeation of cell penetrating peptides into skin. European Journal of Pharmaceutics and Biopharmaceutics, 86, 190–199.
Dietz, G. P., Valbuena, P. C., Dietz, B., Meuer, K., Mueller, P., Weishaupt, J. H., et al. (2006). Application of a blood-brain-barrier-penetrating form of GDNF in a mouse model for Parkinson’s disease. Brain Research, 1082, 61–66.
Ding, Q., Markesbery, W. R., Chen, Q., Li, F., & Keller, J. N. (2005). Ribosome dysfunction is an early event in Alzheimer’s disease. Journal of Neuroscience, 25, 9171–9175.
Doeppner, T. R., Nagel, F., Dietz, G. P., Weise, J., Tonges, L., Schwarting, S., et al. (2009). TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice. Journal of Cerebral Blood Flow and Metabolism, 29, 1187–1196.
Dominska, M., & Dykxhoorn, D. M. (2010). Breaking down the barriers: siRNA delivery and endosome escape. Journal of Cell Science, 123, 1183–1189.
Dondi, R., Yaghini, E., Tewari, K. M., Wang, L., Giuntini, F., Loizidou, M., et al. (2016). Flexible synthesis of cationic peptide-porphyrin derivatives for light-triggered drug delivery and photodynamic therapy. Organic and Biomolecular Chemistry, 14, 11488–11501.
Doran, P. M. (2013). Therapeutically important proteins from in vitro plant tissue culture systems. Current Medicinal Chemistry, 20, 1047–1055.
Drin, G., Cottin, S., Blanc, E., Rees, A. R., & Temsamani, J. (2003). Studies on the internalization mechanism of cationic cell-penetrating peptides. Journal of Biological Chemistry, 278, 31192–31201.
Drin, G., Rousselle, C., Scherrmann, J. M., Rees, A. R. & Temsamani, J. (2002). Peptide delivery to the brain via adsorptive-mediated endocytosis: Advances with SynB vectors. AAPS PharmSci, 4.
Dube, T., Chibh, S., Mishra, J. & Panda, J. J. (2017). Receptor targeted polymeric nanostructures capable of navigating across the blood-brain barrier for effective delivery of neural therapeutics. ACS Chemical Neuroscience, 25.
Eggenberger, K., Birtalan, E., Schroder, T., Brase, S., & Nick, P. (2009). Passage of Trojan peptoids into plant cells. ChemBioChem, 10, 2504–2512.
Eriste, E., Kurrikoff, K., Suhorutsenko, J., Oskolkov, N., Copolovici, D. M., Jones, S., et al. (2013). Peptide-based glioma-targeted drug delivery vector gHoPe2. Bioconjugate Chemistry, 24, 305–313.
Erlich-Hadad, T., Hadad, R., Feldman, A., Greif, H., Lictenstein, M., & Lorberboum-Galski, H. (2018). TAT-MTS-MCM fusion proteins reduce MMA levels and improve mitochondrial activity and liver function in MCM-deficient cells. Journal of Cellular and Molecular Medicine, 22, 1601–1613.
Eudes, F., & Macmillan, T. (2014). Organelle targeting nanocarriers. Google Patents.
Feng, X., Gao, X., Kang, T., Jiang, D., Yao, J., Jing, Y., et al. (2015). Mammary-derived growth inhibitor targeting peptide-modified PEG-PLA nanoparticles for enhanced targeted glioblastoma therapy. Bioconjugate Chemistry, 26, 1850–1861.
Fillebeen, C., Descamps, L., Dehouck, M. P., Fenart, L., Benaissa, M., Spik, G., et al. (1999). Receptor-mediated transcytosis of lactoferrin through the blood-brain barrier. Journal of Biological Chemistry, 274, 7011–7017.
Fischer, R., Bachle, D., Fotin-Mleczek, M., Jung, G., Kalbacher, H., & Brock, R. (2006). A targeted protease substrate for a quantitative determination of protease activities in the endolysosomal pathway. ChemBioChem, 7, 1428–1434.
Fischer, R., Kohler, K., Fotin-Mleczek, M., & Brock, R. (2004). A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. Journal of Biological Chemistry, 279, 12625–12635.
Fisher, L., Samuelsson, M., Jiang, Y., Ramberg, V., Figueroa, R., Hallberg, E., et al. (2007). Targeting cytokine expression in glial cells by cellular delivery of an NF-kappaB decoy. Journal of Molecular Neuroscience, 31, 209–219.
Foger, F., Kopf, A., Loretz, B., Albrecht, K., & Bernkop-Schnurch, A. (2008). Correlation of in vitro and in vivo models for the oral absorption of peptide drugs. Amino Acids, 35, 233–241.
Fonseca, S. B., Pereira, M. P., Mourtada, R., Gronda, M., Horton, K. L., Hurren, R., et al. (2011). Rerouting chlorambucil to mitochondria combats drug deactivation and resistance in cancer cells. Chemistry and Biology, 18, 445–453.
Fortin, D., Gendron, C., Boudrias, M., & Garant, M. P. (2007). Enhanced chemotherapy delivery by intraarterial infusion and blood-brain barrier disruption in the treatment of cerebral metastasis. Cancer, 109, 751–760.
Frankenburg, S., Grinberg, I., Bazak, Z., Fingerut, L., Pitcovski, J., Gorodetsky, R., et al. (2007). Immunological activation following transcutaneous delivery of HR-gp100 protein. Vaccine, 25, 4564–4570.
Fretz, M. M., Penning, N. A., Al-Taei, S., Futaki, S., Takeuchi, T., Nakase, I., et al. (2007). Temperature-, concentration- and cholesterol-dependent translocation of L- and D-octa-arginine across the plasma and nuclear membrane of CD34+ leukaemia cells. Biochemical Journal, 403, 335–342.
Friden, P. M., Walus, L. R., Musso, G. F., Taylor, M. A., Malfroy, B., & Starzyk, R. M. (1991). Anti-transferrin receptor antibody and antibody-drug conjugates cross the blood-brain barrier. Proceedings of the National Academy of Sciences, 88, 4771–4775.
Fu, A., Wang, Y., Zhan, L., & Zhou, R. (2012). Targeted delivery of proteins into the central nervous system mediated by rabies virus glycoprotein-derived peptide. Pharmaceutical Research, 29, 1562–1569.
Fukuoka, Y., Khafagy, E. S., Goto, T., Kamei, N., Takayama, K., Peppas, N. A., et al. (2018). Combination strategy with complexation hydrogels and cell-penetrating peptides for oral delivery of insulin. Biological &/and Pharmaceutical Bulletin, 41, 811–814.
Furukawa, R., Yamada, Y., Kawamura, E., & Harashima, H. (2015). Mitochondrial delivery of antisense RNA by MITO-Porter results in mitochondrial RNA knockdown, and has a functional impact on mitochondria. Biomaterials, 57, 107–115.
Gaillard, P. J., Visser, C. C., & de Boer, A. G. (2005). Targeted delivery across the blood-brain barrier. Expert Opinion on Drug Delivery, 2, 299–309.
Gaizo, V. D., Mackenzie, J. A., & Payne, R. M. (2003). Targeting proteins to mitochondria using TAT. Molecular Genetics and Metabolism, 80, 170–180.
Gan, H. K., van den Bent, M., Lassman, A. B., Reardon, D. A., & Scott, A. M. (2017). Antibody-drug conjugates in glioblastoma therapy: The right drugs to the right cells. Nature Reviews Clinical Oncology, 4, 95.
Gao, C., Hong, M., Geng, J., Zhou, H., & Dong, J. (2015). Characterization of PI (breast cancer cell special peptide) in MDA-MB-231 breast cancer cells and its potential therapeutic applications. International Journal of Oncology, 47, 1371–1378.
Gao, H., Zhang, S., Cao, S., Yang, Z., Pang, Z., & Jiang, X. (2014). Angiopep-2 and activatable cell-penetrating peptide dual-functionalized nanoparticles for systemic glioma-targeting delivery. Molecular Pharmaceutics, 11, 2755–2763.
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017). Abnormalities of mitochondrial dynamics in neurodegenerative diseases. Antioxidants, 6.
Gao, W., Xiang, B., Meng, T. T., Liu, F., & Qi, X. R. (2013). Chemotherapeutic drug delivery to cancer cells using a combination of folate targeting and tumor microenvironment-sensitive polypeptides. Biomaterials, 34, 4137–4149.
Garcia-Lopez, V., Chen, F., Nilewski, L. G., Duret, G., Aliyan, A., Kolomeisky, A. B., et al. (2017). Molecular machines open cell membranes. Nature, 548, 567–572.
Garcia, J., Fernandez-Blanco, A., Teixido, M., Sanchez-Navarro, M., & Giralt, E. (2018). d-Polyarginine lipopeptides as intestinal permeation enhancers. ChemMedChem.
Gautam, A., Nanda, J. S., Samuel, J. S., Kumari, M., Priyanka, P., Bedi, G., et al. (2016). Topical delivery of protein and peptide using novel cell penetrating peptide IMT-P8. Scientific Reports, 6.
Gehrmann, M., Stangl, S., Foulds, G. A., Oellinger, R., Breuninger, S., Rad, R., et al. (2014). Tumor imaging and targeting potential of an Hsp70-derived 14-mer peptide. PLoS ONE, 9, e105344.
Geisler, I. M., & Chmielewski, J. (2011). Dimeric cationic amphiphilic polyproline helices for mitochondrial targeting. Pharmaceutical Research, 28, 2797–2807.
Gennari, C. G., Franze, S., Pellegrino, S., Corsini, E., Vistoli, G., Montanari, L., et al. (2016). Skin penetrating peptide as a tool to enhance the permeation of heparin through human epidermis. Biomacromolecules, 17, 46–55.
Gerard, G. M. D. S., & Volkmar, W. (2004). Approaches to mitochondrial gene therapy. Current Gene Therapy, 4, 317–328.
Golestanipour, A., Nikkhah, M., Aalami, A., & Hosseinkhani, S. (2018). Gene delivery to tobacco root cells with single-walled carbon nanotubes and cell-penetrating fusogenic peptides. Molecular Biotechnology.
Gonias, S. L., & Campana, W. M. (2014). LDL receptor-related protein-1: A regulator of inflammation in atherosclerosis, cancer, and injury to the nervous system. American Journal of Pathology, 184, 18–27.
Gopalakrishnan, S., Pandey, N., Tamiz, A. P., Vere, J., Carrasco, R., Somerville, R., et al. (2009). Mechanism of action of ZOT-derived peptide AT-1002, a tight junction regulator and absorption enhancer. International Journal of Pharmaceutics, 365, 121–130.
Gorman, G. S., Chinnery, P. F., Dimauro, S., Hirano, M., Koga, Y., Mcfarland, R., et al. (2016). Nature Reviews Disease Primers, 2:16080 10.1038/nrdp.2016.80.
Gotanda, Y., Wei, F. Y., Harada, H., Ohta, K., Nakamura, K., Tomizawa, K., et al. (2014). Efficient transduction of 11 poly-arginine peptide in an ischemic lesion of mouse brain. Journal of Stroke and Cerebrovascular Diseases, 23, 2023–2030.
Goun, E. A., Shinde, R., Dehnert, K. W., Adams-Bond, A., Wender, P. A., Contag, C. H., et al. (2006). Intracellular cargo delivery by an octaarginine transporter adapted to target prostate cancer cells through cell surface protease activation. Bioconjugate Chemistry, 17, 787–796.
Govindarajan, S., Sivakumar, J., Garimidi, P., Rangaraj, N., Kumar, J. M., Rao, N. M., et al. (2012). Targeting human epidermal growth factor receptor 2 by a cell-penetrating peptide-affibody bioconjugate. Biomaterials, 33, 2570–2582.
Griffin, J. I., Cheng, S. K. K., Hayashi, T., Carson, D., Saraswathy, M., Nair, D. P., et al. (2017). Cell-penetrating peptide CGKRK mediates efficient and widespread targeting of bladder mucosa following focal injury. Nanomedicine (Lond), 13, 1925–1932.
Gronewold, A., Horn, M., & Neundorf, I. (2018). Design and biological characterization of novel cell-penetrating peptides preferentially targeting cell nuclei and subnuclear regions. Beilstein Journal of Organic Chemistry, 14, 1378–1388.
Gross, A., Alborzinia, H., Piantavigna, S., Martin, L. L., Wolfl, S., & Metzler-Nolte, N. (2015). Vesicular disruption of lysosomal targeting organometallic polyarginine bioconjugates. Metallomics, 7, 371–384.
Gul, R., Ahmed, N., Shah, K. U., Khan, G. M., & Ur Rehman, A. (2017). Functionalized nanostructures for transdermal delivery of drug cargos. Journal of Drug Targeting, 31, 1–30.
Gupta, S., Jain, A., Chakraborty, M., Sahni, J. K., Ali, J., & Dang, S. (2013). Oral delivery of therapeutic proteins and peptides: A review on recent developments. Drug Delivery, 20, 237–246.
Gupta, U., Kumar, H., Mishra, G., Kumar Sharma, A., Gothwal, A. & Kesharwani, P. (2017). Intranasal drug delivery: A non-invasive approach for the better delivery of neurotherapeutics. Pharmaceutical Nanotechnology, 14, 2211738505666170515113936.
Haeckel, A., Appler, F., Ariza de Schellenberger, A., & Schellenberger, E. (2016). XTEN as biological alternative to PEGylation allows complete expression of a protease-activatable killin-based cytostatic. PLoS One, 11.
Han, S. S., Li, Z. Y., Zhu, J. Y., Han, K., Zeng, Z. Y., Hong, W., et al. (2015). Dual-pH sensitive charge-reversal polypeptide micelles for tumor-triggered targeting uptake and nuclear drug delivery. Small (Weinheim an der Bergstrasse, Germany), 11, 2543–2554.
Hansen, A., Schafer, I., Knappe, D., Seibel, P., & Hoffmann, R. (2012). Intracellular toxicity of proline-rich antimicrobial peptides shuttled into mammalian cells by the cell-penetrating peptide penetratin. Antimicrobial Agents and Chemotherapy, 56, 5194–5201.
Hansen, M., Kilk, K., & Langel, Ü. (2008). Predicting cell-penetrating peptides. Advanced Drug Delivery Reviews, 60, 572–579.
Harada, H., Hiraoka, M., & Kizaka-Kondoh, S. (2002). Antitumor effect of TAT-oxygen-dependent degradation-caspase-3 fusion protein specifically stabilized and activated in hypoxic tumor cells. Cancer Research, 62, 2013–2018.
Hariton-Gazal, E., Rosenbluh, J., Graessmann, A., Gilon, C., & Loyter, A. (2003). Direct translocation of histone molecules across cell membranes. Journal of Cell Science, 116, 4577–4586.
Harris, T. J., von Maltzahn, G., Lord, M. E., Park, J. H., Agrawal, A., Min, D. H., et al. (2008). Protease-triggered unveiling of bioactive nanoparticles. Small (Weinheim an der Bergstrasse, Germany), 4, 1307–1312.
Hart, M. R., Su, H. Y., Broka, D., Goverdhan, A., & Schroeder, J. A. (2013). Inactive ERBB receptors cooperate with reactive oxygen species to suppress cancer progression. Molecular Therapy, 21, 1996–2007.
Hatakeyama, H., Akita, H., Ito, E., Hayashi, Y., Oishi, M., Nagasaki, Y., et al. (2011). Systemic delivery of siRNA to tumors using a lipid nanoparticle containing a tumor-specific cleavable PEG-lipid. Biomaterials, 32, 4306–4316.
Hayashi, Y., Mizuno, R., Ikramy, K. A., Akita, H., & Harashima, H. (2012). Pretreatment of hepatocyte growth factor gene transfer mediated by octaarginine peptide-modified nanoparticles ameliorates LPS/D-galactosamine-induced hepatitis. Nucleic Acid Therapeutics, 22, 360–363.
Hayashi, Y., Yamauchi, J., Khalil, I. A., Kajimoto, K., Akita, H., & Harashima, H. (2011). Cell penetrating peptide-mediated systemic siRNA delivery to the liver. International Journal of Pharmaceutics, 419, 308–313.
He, H., Sun, L., Ye, J., Liu, E., Chen, S., Liang, Q., et al. (2016). Enzyme-triggered, cell penetrating peptide-mediated delivery of anti-tumor agents. Journal of Controlled Release, 240, 67–76.
Held, A., Glas, A., Dietrich, L., Bollmann, M., Brandstadter, K., Grossmann, T. N., et al. (2018). Targeting beta-catenin dependent Wnt signaling via peptidomimetic inhibitors in murine chondrocytes and OA cartilage. Osteoarthritis Cartilage.
Herce, H. D., Schumacher, D., Schneider, A. F. L., Ludwig, A. K., Mann, F. A., Fillies, M., et al. (2017). Cell-permeable nanobodies for targeted immunolabelling and antigen manipulation in living cells. Nature Chemistry, 9, 762–771.
Herve, F., Ghinea, N., & Scherrmann, J. M. (2008). CNS delivery via adsorptive transcytosis. American Association of Pharmaceutical Scientists Journal, 10, 455–472.
Hida, K., Maishi, N., Sakurai, Y., Hida, Y., & Harashima, H. (2016). Heterogeneity of tumor endothelial cells and drug delivery. Advanced Drug Delivery Reviews, 99, 140–147.
Hingorani, D. V., Lemieux, A. J., Acevedo, J. R., Glasgow, H. L., Kedarisetty, S., Whitney, M. A., et al. (2017). Early detection of squamous cell carcinoma in carcinogen induced oral cancer rodent model by ratiometric activatable cell penetrating peptides. Oral Oncology, 71, 156–162.
Hofbauer, A., Peters, J., Arcalis, E., Rademacher, T., Lampel, J., Eudes, F., et al. (2014). The induction of recombinant protein bodies in different subcellular compartments reveals a cryptic plastid-targeting signal in the 27-kDa γ-Zein sequence. Frontiers in Bioengineering and Biotechnology, 2, 67.
Holm, T., Netzereab, S., Hansen, M., Langel, Ü., & Hällbrink, M. (2005). Uptake of cell-penetrating peptides in yeasts. FEBS Letters, 579, 5217–5222.
Hossain, M. K., Cho, H. Y., Kim, K. J., & Choi, J. W. (2015). In situ monitoring of doxorubicin release from biohybrid nanoparticles modified with antibody and cell-penetrating peptides in breast cancer cells using surface-enhanced Raman spectroscopy. Biosensors and Bioelectronics, 71, 300–305.
Hossen, M. N., Kajimoto, K., Akita, H., Hyodo, M., & Harashima, H. (2012). Vascular-targeted nanotherapy for obesity: Unexpected passive targeting mechanism to obese fat for the enhancement of active drug delivery. Journal of Control Release, 163, 101–110.
Hsu, T., & Mitragotri, S. (2011). Delivery of siRNA and other macromolecules into skin and cells using a peptide enhancer. Proceedings of the National Academy of Sciences USA, 108, 15816–15821.
Huang, R., Li, J., Kebebe, D., Wu, Y., Zhang, B., & Liu, Z. (2018). Cell penetrating peptides functionalized gambogic acid-nanostructured lipid carrier for cancer treatment. Drug Delivery, 25, 757–765.
Huang, S., Shao, K., Kuang, Y., Liu, Y., Li, J., An, S., et al. (2013a). Tumor targeting and microenvironment-responsive nanoparticles for gene delivery. Biomaterials, 34, 5294–5302.
Huang, S., Shao, K., Liu, Y., Kuang, Y., Li, J., An, S., et al. (2013b). Tumor-targeting and microenvironment-responsive smart nanoparticles for combination therapy of antiangiogenesis and apoptosis. ACS Nano, 7, 2860–2871.
Huang, Y., Park, Y. S., Wang, J., Moon, C., Kwon, Y. M., Chung, H. S., et al. (2010). ATTEMPTS system: A macromolecular prodrug strategy for cancer drug delivery. Current Pharmaceutical Design, 16, 2369–2376.
Huber, J. D., Egleton, R. D., & Davis, T. P. (2001). Molecular physiology and pathophysiology of tight junctions in the blood-brain barrier. Trends in Neurosciences, 24, 719–725.
Hunt, H., Simon-Gracia, L., Tobi, A., Kotamraju, V. R., Sharma, S., Nigul, M., et al. (2017). Targeting of p32 in peritoneal carcinomatosis with intraperitoneal linTT1 peptide-guided pro-apoptotic nanoparticles. Journal of Control Release, 260, 142–153.
Hussain, T., Mastrodimos, M. B., Raju, S. C., Glasgow, H. L., Whitney, M., Friedman, B., et al. (2015). Fluorescently labeled peptide increases identification of degenerated facial nerve branches during surgery and improves functional outcome. PLoS One, 10.
Hyman, J. M., Geihe, E. I., Trantow, B. M., Parvin, B., & Wender, P. A. (2012). A molecular method for the delivery of small molecules and proteins across the cell wall of algae using molecular transporters. Proceedings of the National Academy of Sciences USA, 109, 13225–13230.
Hyvonen, M., Enbäck, J., Huhtala, T., Lammi, J., Sihto, H., Weisell, J., et al. (2014). Novel target for peptide-based imaging and treatment of brain tumors. Molecular Cancer Therapeutics, 13, 996–1007.
Hällbrink, M., & Karelson, M. (2015). Prediction of cell-penetrating peptides. Methods Mol Biol, 1324, 39–58.
Hällbrink, M., Kilk, K., Elmquist, A., Lundberg, P., Lindgren, M., Jiang, Y., et al. (2005). Prediction of cell-penetrating peptides. International Journal of Peptide Research and Therapeutics, 11, 249–259.
Hällbrink, M., Kilk, K., Lundberg, P., Soomets, U., Elmquist, A., Zorko, M., et al. (2002). Cell-penetrating peptides. PCT WO2003106491.
Im, J., Das, S., Jeong, D., Kim, C. J., Lim, H. S., Kim, K. H., et al. (2017). Intracellular and transdermal protein delivery mediated by non-covalent interactions with a synthetic guanidine-rich molecular carrier. International Journal of Pharmaceutics, 528, 646–654.
Immordino, M. L., Dosio, F., & Cattel, L. (2006). Stealth liposomes: Review of the basic science, rationale, and clinical applications, existing and potential. International Journal of Nanomedicine, 1, 297–315.
Ishiguro, S., Alhakamy, N. A., Uppalapati, D., Delzeit, J., Berkland, C. J., & Tamura, M. (2017). Combined local pulmonary and systemic delivery of AT2R gene by modified TAT peptide nanoparticles attenuates both murine and human lung carcinoma xenografts in Mice. Journal of Pharmaceutical Sciences, 106, 385–394.
Ishikawa, T., Somiya, K., Munechika, R., Harashima, H., & Yamada, Y. (2018). Mitochondrial transgene expression via an artificial mitochondrial DNA vector in cells from a patient with a mitochondrial disease. Journal of Controlled Release.
Iwasaki, T., Tokuda, Y., Kotake, A., Okada, H., Takeda, S., Kawano, T., et al. (2015). Cellular uptake and in vivo distribution of polyhistidine peptides. Journal of Controlled Release, 210, 115–124.
Iwase, Y., Kamei, N., Khafagy el, S., Miyamoto, M., & Takeda-Morishita, M. (2016). Use of a non-covalent cell-penetrating peptide strategy to enhance the nasal delivery of interferon beta and its PEGylated form. International Journal of Pharmaceutics, 510, 304–310.
Jacq, A., Burlat, V., & Jamet, E. (2017). Plant cell wall proteomics as a strategy to reveal candidate proteins involved in extracellular lipid metabolism. Current Protein and Peptide Science.
Jagtap, U. B., Gurav, R. G., & Bapat, V. A. (2011). Role of RNA interference in plant improvement. Die Naturwissenschaften, 98, 473–492.
Jain, A., & Chugh, A. (2016). Mitochondrial transit peptide exhibits cell penetration ability and efficiently delivers macromolecules to mitochondria. FEBS Letters, 590, 2896–2905.
Jain, A., Yadav, B. K., & Chugh, A. (2015). Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. The FEBS Journal, 282, 732–745.
Jain, M., Chauhan, S. C., Singh, A. P., Venkatraman, G., Colcher, D., & Batra, S. K. (2005). Penetratin improves tumor retention of single-chain antibodies: A novel step toward optimization of radioimmunotherapy of solid tumors. Cancer Research, 65, 7840–7846.
Jarvinen, T. A., May, U., & Prince, S. (2015). Systemically administered, target organ-specific therapies for regenerative medicine. International Journal of Molecular Sciences, 16, 23556–23571.
Jarvinen, T. A. H., & Ruoslahti, E. (2018). Generation of multi-functional target organ specific anti-fibrotic molecule by molecular engineering of the extracellular matrix protein, decorin. British Journal of Pharmacology.
Jean, S. R., Ahmed, M., Lei, E. K., Wisnovsky, S. P., & Kelley, S. O. (2016). Peptide-mediated delivery of chemical probes and therapeutics to mitochondria. Accounts of Chemical Research, 49, 1893–1902.
Jeong, E. J., Choi, M., Lee, J., Rhim, T., & Lee, K. Y. (2015). The spacer arm length in cell-penetrating peptides influences chitosan/siRNA nanoparticle delivery for pulmonary inflammation treatment. Nanoscale, 7, 20095–20104.
Jeong, J. H., Kim, K., Lim, D., Jeong, K., Hong, Y., Nguyen, V. H., et al. (2014). Anti-tumoral effect of the mitochondrial target domain of Noxa delivered by an engineered Salmonella typhimurium. PLoS One, 9, e80050.
Jeyarajan, S., Xavier, J., Rao, N. M., & Gopal, V. (2010). Plasmid DNA delivery into MDA-MB-453 cells mediated by recombinant Her-NLS fusion protein. International Journal of Nanomedicine, 5, 725–733.
Ji, T., Ding, Y., Zhao, Y., Wang, J., Qin, H., Liu, X., et al. (2015). Peptide assembly integration of fibroblast-targeting and cell-penetration features for enhanced antitumor drug delivery. Advanced Materials, 27, 1865–1873.
Jiang, T., Olson, E. S., Nguyen, Q. T., Roy, M., Jennings, P. A., & Tsien, R. Y. (2004). Tumor imaging by means of proteolytic activation of cell-penetrating peptides. Proceedings of the National Academy of Sciences USA, 101, 17867–17872.
Jiang, T., Wang, T., Li, T., Ma, Y., Shen, S., He, B., et al. (2018). Enhanced transdermal drug delivery by transfersome-embedded oligopeptide hydrogel for topical chemotherapy of melanoma. ACS Nano.
Jiang, T., Zhang, Z., Zhang, Y., Lv, H., Zhou, J., Li, C., et al. (2012). Dual-functional liposomes based on pH-responsive cell-penetrating peptide and hyaluronic acid for tumor-targeted anticancer drug delivery. Biomaterials, 33, 9246–9258.
Jin, E., Zhang, B., Sun, X., Zhou, Z., Ma, X., Sun, Q., et al. (2013). Acid-active cell-penetrating peptides for in vivo tumor-targeted drug delivery. Journal of the American Chemical Society, 135, 933–940.
Jo, E., Heo, J. S., Lim, J. Y., Lee, B. R., Yoon, C. J., Kim, J., et al. (2018). Peptide ligand-mediated endocytosis of nanoparticles to cancer cells: Cell receptor-binding- versus cell membrane-penetrating peptides. Biotechnology and Bioengineering.
Johnson, L. N., Cashman, S. M., Read, S. P., & Kumar-Singh, R. (2010). Cell penetrating peptide POD mediates delivery of recombinant proteins to retina, cornea and skin. Vision Research, 50, 686–697.
Juks, C., Padari, K., Margus, H., Kriiska, A., Etverk, I., Arukuusk, P., et al. (2015). The role of endocytosis in the uptake and intracellular trafficking of PepFect14-nucleic acid nanocomplexes via class A scavenger receptors. Biochimica et Biophysica Acta (BBA)-Biomembranes, 12, 25.
Jun, H. R., Pham, C. D., Lim, S. I., Lee, S. C., Kim, Y. S., Park, S., et al. (2010). An RNA-hydrolyzing recombinant antibody exhibits an antiviral activity against classical swine fever virus. Biochemical and Biophysical Research Communications, 395, 484–489.
Kagawa, Y., Inoki, Y., & Endo, H. (2001). Gene therapy by mitochondrial transfer. Advanced Drug Delivery Reviews, 49, 107–119.
Kalafut, D., Anderson, T. N., & Chmielewski, J. (2012). Mitochondrial targeting of a cationic amphiphilic polyproline helix. Bioorganic and Medicinal Chemistry Letters, 22, 561–563.
Kamei, N., Khafagy, E. S., Hirose, J. & Takeda-Morishita, M. (2017a). Potential of single cationic amino acid molecule “Arginine” for stimulating oral absorption of insulin. International Journal of Pharmaceutics, 18, 30075-3.
Kamei, N., Nielsen, E. J., Khafagy el, S., & Takeda-Morishita, M. (2013). Noninvasive insulin delivery: The great potential of cell-penetrating peptides. Therapeutic Delivery, 4, 315–326.
Kamei, N., & Takeda-Morishita, M. (2015). Brain delivery of insulin boosted by intranasal coadministration with cell-penetrating peptides. Journal of Controlled Release, 197, 105–110.
Kamei, N., Tanaka, M., Choi, H., Okada, N., Ikeda, T., Itokazu, R., et al. (2017b). Effect of an enhanced nose-to-brain delivery of insulin on mild and progressive memory loss in the senescence-accelerated mouse. Molecular Pharmaceutics, 14, 916–927.
Kamei, N., Yamaoka, A., Fukuyama, Y., Itokazu, R., & Takeda-Morishita, M. (2018). Noncovalent strategy with cell-penetrating peptides to facilitate the brain delivery of insulin through the blood-brain barrier. Biological and Pharmaceutical Bulletin, 41, 546–554.
Kanazawa, T. (2015). Brain delivery of small interfering ribonucleic acid and drugs through intranasal administration with nano-sized polymer micelles. Medical devices (Auckland, NZ), 8, 57–64.
Kanazawa, T., Akiyama, F., Kakizaki, S., Takashima, Y., & Seta, Y. (2013). Delivery of siRNA to the brain using a combination of nose-to-brain delivery and cell-penetrating peptide-modified nano-micelles. Biomaterials, 34, 9220–9226.
Kanazawa, T., Morisaki, K., Suzuki, S., & Takashima, Y. (2014). Prolongation of life in rats with malignant glioma by intranasal siRNA/drug codelivery to the brain with cell-penetrating peptide-modified micelles. Molecular Pharmaceutics, 11, 1471–1478.
Kang, Y. C., Son, M., Kang, S., Im, S., Piao, Y., Lim, K. S., et al. (2018). Cell-penetrating artificial mitochondria-targeting peptide-conjugated metallothionein 1A alleviates mitochondrial damage in Parkinson’s disease models. Experimental & Molecular Medicine, 50, 105.
Kastin, A. J., & Pan, W. (2016). Involvement of the blood-brain barrier in metabolic regulation. CNS & Neurological Disorders-Drug Targets, 15, 1118–1128.
Kawabata, A., Baoum, A., Ohta, N., Jacquez, S., Seo, G. M., Berkland, C., et al. (2012). Intratracheal administration of a nanoparticle-based therapy with the angiotensin II type 2 receptor gene attenuates lung cancer growth. Cancer Research, 72, 2057–2067.
Ke, A. Q., Liu, A. D., Gao, Y. N., Luo, D. N., Li, Z. F., Yu, Y. Q., et al. (2018). Development of novel affinity reagents for detecting protein tyrosine phosphorylation based on superbinder SH2 domain in tumor cells. Analytica Chimica Acta, 1032, 138–146.
Ke, W., Shao, K., Huang, R., Han, L., Liu, Y., Li, J., et al. (2009). Gene delivery targeted to the brain using an Angiopep-conjugated polyethyleneglycol-modified polyamidoamine dendrimer. Biomaterials, 30, 6976–6985.
Khafagy el, S., Iwamae, R., Kamei, N., & Takeda-Morishita, M. (2015). Region-dependent role of cell-penetrating peptides in insulin absorption across the rat small intestinal membrane. The AAPS journal, 17, 1427–1437.
Khafagy el, S., Morishita, M., Isowa, K., Imai, J., & Takayama, K. (2009). Effect of cell-penetrating peptides on the nasal absorption of insulin. Journal of Controlled Release, 133, 103–108.
Khalil, I. A., Hayashi, Y., Mizuno, R., & Harashima, H. (2011). Octaarginine- and pH sensitive fusogenic peptide-modified nanoparticles for liver gene delivery. Journal of Controlled Release, 156, 374–380.
Khalily, M. P., Gerekci, S., Gulec, E. A., Ozen, C., & Ozcubukcu, S. (2018). Structure-based design, synthesis and anticancer effect of cyclic Smac-polyarginine peptides. Amino Acids.
Khan, A. R., Liu, M., Khan, M. W., & Zhai, G. (2017). Progress in brain targeting drug delivery system by nasal route. Journal of Controlled Release, 5, 30825–30828.
Kim, B. K., Kang, H., Doh, K. O., Lee, S. H., Park, J. W., Lee, S. J., et al. (2012). Homodimeric SV40 NLS peptide formed by disulfide bond as enhancer for gene delivery. Bioorganic & Medicinal Chemistry Letters, 22, 5415–5418.
Kim, G. C., Ahn, J. H., Oh, J. H., Nam, S., Hyun, S., Yu, J., et al. (2018a). Photoswitching of cell penetration of amphipathic peptides by control of alpha-helical conformation. Biomacromolecules.
Kim, J. S., Park, J. Y., Shin, S. M., Park, S. W., Jun, S. Y., Hong, J. S., et al. (2018b). Engineering of a tumor cell-specific, cytosol-penetrating antibody with high endosomal escape efficacy. Biochemical and Biophysical Research Communications, 503, 2510–2516.
Kim, Y., Lillo, A. M., Steiniger, S. C., Liu, Y., Ballatore, C., Anichini, A., et al. (2006). Targeting heat shock proteins on cancer cells: Selection, characterization, and cell-penetrating properties of a peptidic GRP78 ligand. Biochemistry, 45, 9434–9444.
Kim, Y. H., Han, M. E., & Oh, S. O. (2017). The molecular mechanism for nuclear transport and its application. Anatomy & Cell Biology, 50, 77–85.
Kimura, S., Kawano, T., & Iwasaki, T. (2017). Short polyhistidine peptides penetrate effectively into Nicotiana tabacum-cultured cells and Saccharomyces cerevisiae cells. Bioscience, Biotechnology, and Biochemistry, 81, 112–118.
Kobayashi, N., Niwa, M., Hao, Y., & Yoshida, T. (2010). Nucleolar localization signals of LIM kinase 2 function as a cell-penetrating peptide. Protein and Peptide Letters, 17, 1480–1488.
Kreuter, J., Hekmatara, T., Dreis, S., Vogel, T., Gelperina, S., & Langer, K. (2007). Covalent attachment of apolipoprotein A-I and apolipoprotein B-100 to albumin nanoparticles enables drug transport into the brain. Journal of Controlled Release, 118, 54–58.
Kristensen, M., Birch, D., & Mörck Nielsen, H. (2016). Applications and challenges for use of cell-penetrating peptides as delivery vectors for peptide and protein cargos. International Journal of Molecular Sciences, 17, pii: E185.
Kumagai, A. K., Eisenberg, J. B., & Pardridge, W. M. (1987). Absorptive-mediated endocytosis of cationized albumin and a beta-endorphin-cationized albumin chimeric peptide by isolated brain capillaries. Model system of blood-brain barrier transport. Journal of Biological Chemistry, 262, 15214–15219.
Kumar, P., Ban, H. S., Kim, S. S., Wu, H., Pearson, T., Greiner, D. L., et al. (2008). T cell-specific siRNA delivery suppresses HIV-1 infection in humanized mice. Cell, 134, 577–586.
Kumar, P., Wu, H., McBride, J. L., Jung, K. E., Kim, M. H., Davidson, B. L., et al. (2007). Transvascular delivery of small interfering RNA to the central nervous system. Nature, 448, 39–43.
Kumar, S., Narishetty, S. T., & Tummala, H. (2015a). Peptides as skin penetration enhancers for low molecular weight drugs and macromolecules. In N. Dragicevic & H. I. Maibach (Eds.) Percutaneous penetration enhancers chemical methods in penetration enhancement: Modification of the Stratum Corneum. Heidelberg: Springer.
Kumar, S., Sahdev, P., Perumal, O., & Tummala, H. (2012). Identification of a novel skin penetration enhancement peptide by phage display peptide library screening. Molecular Pharmaceutics, 9, 1320–1330.
Kumar, S., Zakrewsky, M., Chen, M., Menegatti, S., Muraski, J. A., & Mitragotri, S. (2015b). Peptides as skin penetration enhancers: Mechanisms of action. Journal of Controlled Release, 199, 168–178.
Kumaraswamy, A., Mamidi, A., Desai, P., Sivagnanam, A., Revathi Perumalsamy, L., Ramakrishnan, C., Gromiha, M., et al. (2018). The non-enzymatic RAS effector RASSF7 inhibits oncogenic c-Myc function. Journal of Biological Chemistry.
Kurzrock, R., Gabrail, N., Chandhasin, C., Moulder, S., Smith, C., Brenner, A., et al. (2012). Safety, pharmacokinetics, and activity of GRN1005, a novel conjugate of angiopep-2, a peptide facilitating brain penetration, and paclitaxel, in patients with advanced solid tumors. Molecular Cancer Therapeutics, 11, 308–316.
Kusumoto, K., Akita, H., Ishitsuka, T., Matsumoto, Y., Nomoto, T., Furukawa, R., et al. (2013). Lipid envelope-type nanoparticle incorporating a multifunctional peptide for systemic siRNA delivery to the pulmonary endothelium. ACS Nano, 7, 7534–7541.
Kwon, K. C., & Daniell, H. (2016). Oral delivery of protein drugs bioencapsulated in plant cells. Molecular Therapy, 24, 1342–1350.
Laakkonen, P., Porkka, K., Hoffman, J. A., & Ruoslahti, E. (2002). A tumor-homing peptide with a targeting specificity related to lymphatic vessels. Nature Medicine, 8, 751–755.
Lakkadwala, S., & Singh, J. (2018). Dual functionalized 5-fluorouracil liposomes as highly efficient nanomedicine for glioblastoma treatment as assessed in an in vitro brain tumor model. Journal of Pharmaceutical Sciences.
Lakshmanan, M., Kodama, Y., Yoshizumi, T., Sudesh, K., & Numata, K. (2013). Rapid and efficient gene delivery into plant cells using designed peptide carriers. Biomacromolecules, 14, 10–16.
Lam, J. K., Liang, W., & Chan, H. K. (2012). Pulmonary delivery of therapeutic siRNA. Advanced Drug Delivery Reviews, 64, 1–15.
Larue, B., Hogg, E., Sagare, A., Jovanovic, S., Maness, L., Maurer, C., et al. (2004). Method for measurement of the blood-brain barrier permeability in the perfused mouse brain: Application to amyloid-beta peptide in wild type and Alzheimer’s Tg2576 mice. Journal of Neuroscience Methods, 138, 233–242.
Lee, E. S., Gao, Z., Kim, D., Park, K., Kwon, I. C., & Bae, Y. H. (2008a). Super pH-sensitive multifunctional polymeric micelle for tumor pH(e) specific TAT exposure and multidrug resistance. Journal of Controlled Release, 129, 228–236.
Lee, H. S., Park, C. B., Kim, J. M., Jang, S. A., Park, I. Y., Kim, M. S., et al. (2008b). Mechanism of anticancer activity of buforin IIb, a histone H2A-derived peptide. Cancer Letters, 271, 47–55.
Lee, W. R., Jang, J. Y., Kim, J. S., Kwon, M. H., & Kim, Y. S. (2010). Gene silencing by cell-penetrating, sequence-selective and nucleic-acid hydrolyzing antibodies. Nucleic Acids Research, 38, 1596–1609.
Lei, E. K., & Kelley, S. O. (2017). Delivery and release of small-molecule probes in mitochondria using traceless linkers. Journal of the American Chemical Society, 139, 9455–9458.
Letoha, T., Kusz, E., Papai, G., Szabolcs, A., Kaszaki, J., Varga, I., et al. (2006). In vitro and in vivo nuclear factor-kappaB inhibitory effects of the cell-penetrating penetratin peptide. Molecular Pharmacology, 69, 2027–2036.
Li, H., He, J., Yi, H., Xiang, G., Chen, K., et al. (2015). siRNA suppression of hTERT using activatable cell-penetrating peptides in hepatoma cells. Bioscience Reports, 35.
Li, L., Geisler, I., Chmielewski, J., & Cheng, J. X. (2010). Cationic amphiphilic polyproline helix P11LRR targets intracellular mitochondria. Journal of Controlled Release, 142, 259–266.
Li, T., Bourgeois, J. P., Celli, S., Glacial, F., le Sourd, A. M., Mecheri, S., et al. (2012). Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: Application to brain imaging. The FASEB Journal, 26, 3969–3979.
Li, X., Tsibouklis, J., Weng, T., Zhang, B., Yin, G., Feng, G., et al. (2017). Nano carriers for drug transport across the blood-brain barrier. Journal of Drug Targeting, 25, 17–28.
Lightowlers, R. N., Taylor, R. W., & Turnbull, D. M. (2015). Mutations causing mitochondrial disease: What is new and what challenges remain? Science, 349, 1494–1499.
Lim, K. J., Sung, B. H., Shin, J. R., Lee, Y. W., Kim DA, J., Yang, K. S., et al. (2013). A cancer specific cell-penetrating peptide, BR2, for the efficient delivery of an scFv into cancer cells. PLoS One, 8, e66084.
Lin, C. M., Huang, K., Zeng, Y., Chen, X. C., Wang, S., & Li, Y. (2012). A simple, noninvasive and efficient method for transdermal delivery of siRNA. Archives of Dermatological Research, 304, 139–144.
Lin, R., Zhang, P., Cheetham, A. G., Walston, J., Abadir, P., & Cui, H. (2015). Dual peptide conjugation strategy for improved cellular uptake and mitochondria targeting. Bioconjugate Chemistry, 26, 71–77.
Lin, S. Y., Chen, N. T., Sum, S. P., Lo, L. W., & Yang, C. S. (2008). Ligand exchanged photoluminescent gold quantum dots functionalized with leading peptides for nuclear targeting and intracellular imaging. Chemical Communications, 21, 4762–4764.
Lin, T., Liu, E., He, H., Shin, M. C., Moon, C., Yang, V. C., et al. (2016a). Nose-to-brain delivery of macromolecules mediated by cell-penetrating peptides. Acta Pharmaceutica Sinica B, 6, 352–358.
Lin, T., Zhao, P., Jiang, Y., Tang, Y., Jin, H., Pan, Z., et al. (2016b). Blood-brain-barrier-penetrating albumin nanoparticles for biomimetic drug delivery via albumin-binding protein pathways for antiglioma therapy. ACS Nano, 10, 9999–10012.
Lindgren, M. E., Hällbrink, M. M., Elmquist, A. M., & Langel, Ü. (2004). Passage of cell-penetrating peptides across a human epithelial cell layer in vitro. Biochemical Journal, 377, 69–76.
Lippmann, E. S., Azarin, S. M., Kay, J. E., Nessler, R. A., Wilson, H. K., Al-Ahmad, A., et al. (2012). Derivation of blood-brain barrier endothelial cells from human pluripotent stem cells. Nature Biotechnology, 30, 783–791.
Liu, B. R., Chou, J. C., & Lee, H. J. (2008). Cell membrane diversity in noncovalent protein transduction. Journal of Membrane Biology, 222, 1–15.
Liu, B. R., Huang, Y. W., Aronstam, R. S., & Lee, H. J. (2016). Identification of a short cell-penetrating peptide from bovine lactoferricin for intracellular delivery of DNA in human A549 cells. PLoS One, 11.
Liu, C., Liu, X. N., Wang, G. L., Hei, Y., Meng, S., Yang, L. F., et al. (2017a). A dual-mediated liposomal drug delivery system targeting the brain: rational construction, integrity evaluation across the blood-brain barrier, and the transporting mechanism to glioma cells. International Journal of Nanomedicine, 12, 2407–2425.
Liu, C., Yao, S., Li, X., Wang, F., & Jiang, Y. (2017b). iRGD-mediated core-shell nanoparticles loading carmustine and O6-benzylguanine for glioma therapy. Journal of Drug Targeting, 25, 235–246.
Liu, D., Zienkiewicz, J., Digiandomenico, A., & Hawiger, J. (2009a). Suppression of acute lung inflammation by intracellular peptide delivery of a nuclear import inhibitor. Molecular Therapy, 17, 796–802.
Liu, J., Zhang, B., Luo, Z., Ding, X., Li, J., Dai, L., et al. (2015). Enzyme responsive mesoporous silica nanoparticles for targeted tumor therapy in vitro and in vivo. Nanoscale, 7, 3614–3626.
Liu, M.-J., Chou, J.-C., & Lee, H.-J. (2013). A gene delivery method mediated by three arginine-rich cell-penetrating peptides in plant cells. Advanced Studies in Biology, 5, 71–88.
Liu, X., Jiang, J., Nel, A. E., & Meng, H. (2017c). Major effect of transcytosis on nano drug delivery to pancreatic cancer. Molecular & Cellular Oncology, 4.
Liu, X., Wang, Y., & Hnatowich, D. J. (2011). A nanoparticle for tumor targeted delivery of oligomers. Methods Mol Biol, 764, 91–105.
Liu, X., Wang, Y., Nakamura, K., Kawauchi, S., Akalin, A., Cheng, D., et al. (2009b). Auger radiation-induced, antisense-mediated cytotoxicity of tumor cells using a 3-component streptavidin-delivery nanoparticle with 111In. Journal of Nuclear Medicine, 50, 582–590.
Liu, Y., He, X., Kuang, Y., An, S., Wang, C., Guo, Y., et al. (2014). A bacteria deriving peptide modified dendrigraft poly-l-lysines (DGL) self-assembling nanoplatform for targeted gene delivery. Molecular Pharmaceutics, 11, 3330–3341.
Lodish, H., Berk, A., Kaiser, C., Krieger, M., Scott, M., Bretscher, A., et al. (2007). Molecular cell biology (6th ed.) New York: W. H. Freeman and Company.
Lodish, H., Berk, A., & Zipursky, S. (2000). Overview of the secretory pathway. In Molecular cell biology (4th ed.) New York: W. H. Freeman; 2000 section 17.3. Available from: https://www.ncbi.nlm.nih.gov/books/NBK21471/.
Lohcharoenkal, W., Manosaroi, A., Gotz, F., Werner, R. G., Manosroi, W., & Manosaroi, J. (2011). Potent enhancement of GFP uptake into HT-29 cells and rat skin permeation by coincubation with tat peptide. Journal of Pharmaceutical Sciences, 100, 4766–4773.
Long, C., Amoasii, L., Mireault, A. A., McAnally, J. R., Li, H., Sanchez-Ortiz, E., et al. (2016). Postnatal genome editing partially restores dystrophin expression in a mouse model of muscular dystrophy. Science, 351, 400–403.
Lu, S. W., Hu, J. W., Liu, B. R., Lee, C. Y., Li, J. F., Chou, J. C., et al. (2010). Arginine-rich intracellular delivery peptides synchronously deliver covalently and noncovalently linked proteins into plant cells. Journal of Agricultural and Food Chemistry, 58, 2288–2294.
Ludtke, J. J., Zhang, G., Sebestyen, M. G., & Wolff, J. A. (1999). A nuclear localization signal can enhance both the nuclear transport and expression of 1 kb DNA. Journal of Cell Science, 112, 2033–2041.
Lukacs, G. L., Haggie, P., Seksek, O., Lechardeur, D., Freedman, N., & Verkman, A. S. (2000). Size-dependent DNA mobility in cytoplasm and nucleus. Journal of Biological Chemistry, 275, 1625–1629.
Luque-Ortega, J. R., Van’t Hof, W., Veerman, E. C., Saugar, J. M., & Rivas, L. (2008). Human antimicrobial peptide histatin 5 is a cell-penetrating peptide targeting mitochondrial ATP synthesis in Leishmania. The FASEB Journal, 22, 1817–1828.
Lönn, P., Kacsinta, A. D., Cui, X. S., Hamil, A. S., Kaulich, M., Gogoi, K., et al. (2016). Enhancing endosomal escape for intracellular delivery of macromolecular biologic therapeutics. Scientific Reports, 6.
Ma, X. C., Liu, P., Zhang, X. L., Jiang, W. H., Jia, M., Wang, C. X., et al. (2016). Intranasal delivery of recombinant AAV containing BDNF fused with HA2TAT: A potential promising therapy strategy for major depressive disorder. Scientific Reports, 6.
Macdougall, G., Anderton, R. S., Edwards, A. B., Knuckey, N. W., & Meloni, B. P. (2017). The neuroprotective peptide poly-arginine-12 (R12) reduces cell surface levels of NMDA NR2B receptor subunit in cortical neurons; Investigation into the involvement of endocytic mechanisms. Journal of Molecular Neuroscience, 61, 235–246.
Mahmood, A., & Bernkop-Schnurch, A. (2018). SEDDS: A game changing approach for the oral administration of hydrophilic macromolecular drugs. Advanced Drug Delivery Reviews.
Mahmood, A., Prufert, F., Efiana, N. A., Ashraf, M. I., Hermann, M., Hussain, S., et al. (2016). Cell-penetrating self-nanoemulsifying drug delivery systems (SNEDDS) for oral gene delivery. Expert Opinion on Drug Delivery, 13, 1503–1512.
Mallick, S., Thuy, L. T., Lee, S., Park, J. I., & Choi, J. S. (2018). Liposomes containing cholesterol and mitochondria-penetrating peptide (MPP) for targeted delivery of antimycin A to A549 cells. Colloids Surf B Biointerfaces, 161, 356–364.
Manosroi, A., Tangjai, T., Sutthiwanjampa, C., Manosroi, W., Werner, R. G., Gotz, F., et al. (2016). Hypoglycemic activity and stability enhancement of human insulin-tat mixture loaded in elastic anionic niosomes. Drug Delivery, 23, 3157–3167.
Manosroi, J., Lohcharoenkal, W., Gotz, F., Werner, R. G., Manosroi, W., & Manosroi, A. (2014). Novel application of polioviral capsid: development of a potent and prolonged oral calcitonin using polioviral binding ligand and Tat peptide. Drug Development and Industrial Pharmacy, 40, 1092–1100.
Marinova, Z., Vukojevic, V., Surcheva, S., Yakovleva, T., Cebers, G., Pasikova, N., et al. (2005). Translocation of dynorphin neuropeptides across the plasma membrane. A putative mechanism of signal transmission. Journal of Biological Chemistry, 280, 26360–26370.
Martin, R. M., Herce, H. D., Ludwig, A. K., & Cardoso, M. C. (2016). Visualization of the nucleolus in living cells with cell-penetrating fluorescent peptides. Methods Mol Biol, 3792-9_6.
Martin, R. M., Tunnemann, G., Leonhardt, H., & Cardoso, M. C. (2007). Nucleolar marker for living cells. Histochemistry and Cell Biology, 127, 243–251.
McCaffrey, J., McCrudden, C. M., Ali, A. A., Massey, A. S., McBride, J. W., McCrudden, M. T., et al. (2016). Transcending epithelial and intracellular biological barriers; a prototype DNA delivery device. Journal of Controlled Release, 226, 238–247.
McCusker, C. T., Wang, Y., Shan, J., Kinyanjui, M. W., Villeneuve, A., Michael, H., et al. (2007). Inhibition of experimental allergic airways disease by local application of a cell-penetrating dominant-negative STAT-6 peptide. The Journal of Immunology, 179, 2556–2564.
McGowan, J. W., Shao, Q., Vig, P. J., & Bidwell, G. L., III (2016a). Intranasal administration of elastin-like polypeptide for therapeutic delivery to the central nervous system. Drug Design, Development and Therapy, 10, 2803–2813.
McGowan, J. W., Shao, Q., Vig, P. J., & Bidwell, G. L., III (2016b). Intranasal administration of elastin-like polypeptide for therapeutic delivery to the central nervous system. Drug Design, Development and Therapy, 10, 2803–2813.
Mecham, R. P. (1991). Receptors for laminin on mammalian cells. The FASEB Journal, 5, 2538–2546.
Mei, L., Zhang, Q., Yang, Y., He, Q., & Gao, H. (2014). Angiopep-2 and activatable cell penetrating peptide dual modified nanoparticles for enhanced tumor targeting and penetrating. International Journal of Pharmaceutics, 474, 95–102.
Meikle, P. J., Hopwood, J. J., Clague, A. E., & Carey, W. F. (1999). Prevalence of lysosomal storage disorders. JAMA, 281, 249–254.
Melnick, A. (2007). Targeting aggressive B-cell lymphomas with cell-penetrating peptides. Biochemical Society Transactions, 35, 802–806.
Menegatti, S., Zakrewsky, M., Kumar, S., de Oliveira, J. S., Muraski, J. A., & Mitragotri, S. (2016). De Novo design of skin-penetrating peptides for enhanced transdermal delivery of peptide drugs. Advanced Healthcare Materials, 5, 602–609.
Metildi, C. A., Felsen, C. N., Savariar, E. N., Nguyen, Q. T., Kaushal, S., Hoffman, R. M., et al. (2015). Ratiometric activatable cell-penetrating peptides label pancreatic cancer, enabling fluorescence-guided surgery, which reduces metastases and recurrence in orthotopic mouse models. Annals of Surgical Oncology, 22, 2082–2087.
Miyata, K., Ukawa, M., Mohri, K., Fujii, K., Yamada, M., Tanishita, S., et al. (2018). Biocompatible polymers modified with d-octaarginine as an absorption enhancer for nasal peptide delivery. Bioconjugate Chemistry.
Mizuno, T., Miyashita, M., & Miyagawa, H. (2009). Cellular internalization of arginine-rich peptides into tobacco suspension cells: A structure-activity relationship study. Journal of Peptide Science, 15, 259–263.
Mohammed, Y., Teixido, M., Namjoshi, S., Giralt, E., & Benson, H. (2016). Cyclic dipeptide shuttles as a novel skin penetration enhancement approach: Preliminary evaluation with diclofenac. PLoS One, 11.
Mohri, K., Miyata, K., Egawa, T., Tanishita, S., Endo, R., Yagi, H., et al. (2018). Effects of the chemical structures of oligoarginines conjugated to biocompatible polymers as a mucosal adjuvant on antibody induction in nasal cavities. Chemical and Pharmaceutical Bulletin (Tokyo), 66, 375–381.
Mok, H., Bae, K. H., Ahn, C. H., & Park, T. G. (2009). PEGylated and MMP-2 specifically dePEGylated quantum dots: Comparative evaluation of cellular uptake. Langmuir, 25, 1645–1650.
Moktan, S., Perkins, E., Kratz, F., & Raucher, D. (2012). Thermal targeting of an acid-sensitive doxorubicin conjugate of elastin-like polypeptide enhances the therapeutic efficacy compared with the parent compound in vivo. Molecular Cancer Therapeutics, 11, 1547–1556.
Moktan, S., & Raucher, D. (2012). Anticancer activity of proapoptotic peptides is highly improved by thermal targeting using elastin-like polypeptides. International Journal of Peptide Research and Therapeutics, 18, 227–237.
Montrose, K., Yang, Y., & Krissansen, G. W. (2014). The tetrapeptide core of the carrier peptide Xentry is cell-penetrating: Novel activatable forms of Xentry. Scientific Reports, 4, 4900.
Montrose, K., Yang, Y., Sun, X., Wiles, S., & Krissansen, G. W. (2013). Xentry, a new class of cell-penetrating peptide uniquely equipped for delivery of drugs. Scientific Reports, 3, 1661.
Morales, J. O., Fathe, K. R., Brunaugh, A., Ferrati, S., Li, S., Montenegro-Nicolini, M., et al. (2017). Challenges and future prospects for the delivery of biologics: Oral mucosal, pulmonary, and transdermal routes. The AAPS Journal, 19, 652–668.
Morishita, M., Kamei, N., Ehara, J., Isowa, K., & Takayama, K. (2007). A novel approach using functional peptides for efficient intestinal absorption of insulin. Journal of Controlled Release, 118, 177–184.
Morris, M. C., Vidal, P., Chaloin, L., Heitz, F., & Divita, G. (1997). A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Research, 25, 2730–2736.
Moschos, S. A., Jones, S. W., Perry, M. M., Williams, A. E., Erjefalt, J. S., Turner, J. J., et al. (2007a). Lung delivery studies using siRNA conjugated to TAT(48-60) and penetratin reveal peptide induced reduction in gene expression and induction of innate immunity. Bioconjugate Chemistry, 18, 1450–1459.
Moschos, S. A., Williams, A. E., & Lindsay, M. A. (2007b). Cell-penetrating-peptide-mediated siRNA lung delivery. Biochem Soc Trans, 35, 807–810.
Mourtada, R., Fonseca, S. B., Wisnovsky, S. P., Pereira, M. P., Wang, X., Hurren, R., et al. (2013). Re-directing an alkylating agent to mitochondria alters drug target and cell death mechanism. PLoS One, 8.
Muller, R., Misund, K., Holien, T., Bachke, S., Gilljam, K. M., Vatsveen, T. K., et al. (2013). Targeting proliferating cell nuclear antigen and its protein interactions induces apoptosis in multiple myeloma cells. PLoS One, 8, e70430.
Muller, S., Zhao, Y., Brown, T. L., Morgan, A. C., & Kohler, H. (2005). TransMabs: Cell-penetrating antibodies, the next generation. Expert Opinion on Biological Therapy, 5, 237–241.
Muto, K., Kamei, N., Yoshida, M., Takayama, K., & Takeda-Morishita, M. (2016). Cell-penetrating peptide penetratin as a potential tool for developing effective nasal vaccination systems. Journal of Pharmaceutical Sciences, 105, 2014–2017.
Myrberg, H., Lindgren, M., & Langel, Ü. (2007). Protein delivery by the cell-penetrating peptide YTA2. Bioconjugate Chemistry, 18, 170–174.
Myrberg, H., Zhang, L., Mäe, M., & Langel, Ü. (2008). Design of a tumor-homing cell-penetrating peptide. Bioconjugate Chemistry, 19, 70–75.
Mäe, M., Myrberg, H., Jiang, Y., Paves, H., Valkna, A., & Langel, Ü. (2005). Internalisation of cell-penetrating peptides into tobacco protoplasts. Biochimica et Biophysica Acta, 1669, 101–107.
Mäe, M., Rautsi, O., Enbäck, J., Hällbrink, M., Rosenthal-Aizman, K., Lindgren, M., et al. (2012). Tumour targeting with rationally modified cell-penetrating peptides. International Journal of Peptide Research and Therapeutics, 18, 361–371.
Nain, V., Sahi, S., & Verma, A. (2010). CPP-ZFN: a potential DNA-targeting anti-malarial drug. Malaria Journal, 9, 258.
Narla, A., Hurst, S. N., & Ebert, B. L. (2011). Ribosome defects in disorders of erythropoiesis. International Journal of Hematology, 93, 144–149.
Nativo, P., Prior, I. A., & Brust, M. (2008). Uptake and intracellular fate of surface-modified gold nanoparticles. ACS Nano, 2, 1639–1644.
Nekhotiaeva, N., Elmquist, A., Rajarao, G. K., Hällbrink, M., Langel, Ü., & Good, L. (2004). Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides. The FASEB Journal, 18, 394–396.
Neo, S. H., Lew, Q. J., Koh, S. M., Zheng, L., Bi, X., & Chao, S. H. (2016). Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy. Oncotarget, 7, 5483–5494.
Neves-Coelho, S., Eleuterio, R. P., Enguita, F. J., Neves, V., & Castanho, M. (2017). A new noncanonical anionic peptide that translocates a cellular blood-brain barrier model. Molecules, 22.
Nguyen, J., Xie, X., Neu, M., Dumitrascu, R., Reul, R., Sitterberg, J., et al. (2008). Effects of cell-penetrating peptides and pegylation on transfection efficiency of polyethylenimine in mouse lungs. The Journal of Gene Medicine, 10, 1236–1246.
Nguyen, Q. T., Olson, E. S., Aguilera, T. A., Jiang, T., Scadeng, M., Ellies, L. G., et al. (2010). Surgery with molecular fluorescence imaging using activatable cell-penetrating peptides decreases residual cancer and improves survival. Proceedings of the National Academy of Sciences USA, 107, 4317–4322.
Nguyen, Q. T., & Tsien, R. Y. (2013). Fluorescence-guided surgery with live molecular navigation—A new cutting edge. Nature Reviews Cancer, 13, 653–662.
Niazi, A. K., Mileshina, D., Cosset, A., Val, R., Weber-Lotfi, F., & Dietrich, A. (2013). Targeting nucleic acids into mitochondria: Progress and prospects. Mitochondrion, 13, 548–558.
Nielsen, E. J., Kamei, N., & Takeda-Morishita, M. (2015). Safety of the cell-penetrating peptide penetratin as an oral absorption enhancer. Biological and Pharmaceutical Bulletin, 38, 144–146.
Nielsen, E. J., Yoshida, S., Kamei, N., Iwamae, R., Khafagy el, S., Olsen, J., et al. (2014). In vivo proof of concept of oral insulin delivery based on a co-administration strategy with the cell-penetrating peptide penetratin. Journal of Controlled Release, 189, 19–24.
Niu, J., Chu, Y., Huang, Y. F., Chong, Y. S., Jiang, Z. H., Mao, Z. W., et al. (2017). Transdermal gene delivery by functional peptide-conjugated cationic gold nanoparticle reverses the progression and metastasis of cutaneous melanoma. ACS Applied Materials & Interfaces, 9, 9388–9401.
Niu, Z., Samaridou, E., Jaumain, E., Coene, J., Ullio, G., Shrestha, N., et al. (2018). PEG-PGA enveloped octaarginine-peptide nanocomplexes: An oral peptide delivery strategy. Journal of controlled release, 276, 125–139.
Nori, A., & Kopecek, J. (2005). Intracellular targeting of polymer-bound drugs for cancer chemotherapy. Advanced Drug Delivery Reviews, 57, 609–636.
Numata, K., Horii, Y., Oikawa, K., Miyagi, Y., Demura, T., & Ohtani, M. (2018). Library screening of cell-penetrating peptide for BY-2 cells, leaves of Arabidopsis, tobacco, tomato, poplar, and rice callus. Scientific Reports, 8, 10966.
Numata, K., Ohtani, M., Yoshizumi, T., Demura, T., & Kodama, Y. (2014). Local gene silencing in plants via synthetic dsRNA and carrier peptide. Plant Biotechnology Journal, 12, 1027–1034.
Oller-Salvia, B., Sanchez-Navarro, M., Giralt, E., & Teixido, M. (2016). Blood-brain barrier shuttle peptides: An emerging paradigm for brain delivery. Chemical Society Reviews, 45, 4690–4707.
Oller-Salvia, B., Teixido, M., & Giralt, E. (2013). From venoms to BBB shuttles: Synthesis and blood-brain barrier transport assessment of apamin and a nontoxic analog. Biopolymers, 100, 675–686.
Olson, E. S., Aguilera, T. A., Jiang, T., Ellies, L. G., Nguyen, Q. T., Wong, E. H., et al. (2009). In vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer. Integrative Biology (Camb), 1, 382–393.
Olson, E. S., Jiang, T., Aguilera, T. A., Nguyen, Q. T., Ellies, L. G., Scadeng, M., et al. (2010). Activatable cell penetrating peptides linked to nanoparticles as dual probes for in vivo fluorescence and MR imaging of proteases. Proceedings of the National Academy of Sciences USA, 107, 4311–4316.
Olson, E. S., Whitney, M. A., Friedman, B., Aguilera, T. A., Crisp, J. L., Baik, F. M., et al. (2012). In vivo fluorescence imaging of atherosclerotic plaques with activatable cell-penetrating peptides targeting thrombin activity. Integrative Biology (Camb), 4, 595–605.
Orange, J. S., & May, M. J. (2008). Cell penetrating peptide inhibitors of nuclear factor-kappa B. Cellular and Molecular Life Sciences, 65, 3564–3591.
Orihuela, C. J., Mahdavi, J., Thornton, J., Mann, B., Wooldridge, K. G., Abouseada, N., et al. (2009). Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models. The Journal of Clinical Investigation, 119, 1638–1646.
Osman, G., Rodriguez, J., Chan, S. Y., Chisholm, J., Duncan, G., Kim, N., et al. (2018). PEGylated enhanced cell penetrating peptide nanoparticles for lung gene therapy. Journal of Controlled Release, 285, 35–45.
Palm, C., Netzereab, S., & Hallbrink, M. (2006). Quantitatively determined uptake of cell-penetrating peptides in non-mammalian cells with an evaluation of degradation and antimicrobial effects. Peptides, 27, 1710–1716.
Pan, W., & Kastin, A. J. (2016). The blood-brain barrier: regulatory roles in wakefulness and sleep. Neuroscientist, 11, 1073858416639005.
Pan, W., Kastin, A. J., Zankel, T. C., van Kerkhof, P., Terasaki, T., & Bu, G. (2004). Efficient transfer of receptor-associated protein (RAP) across the blood-brain barrier. Journal of Cell Science, 117, 5071–5078.
Pan, Z. Z., Wang, H. Y., Zhang, M., Lin, T. T., Zhang, W. Y., Zhao, P. F., et al. (2016). Nuclear-targeting TAT-PEG-Asp8-doxorubicin polymeric nanoassembly to overcome drug-resistant colon cancer. Acta Pharmacologica Sinica, 37, 1110–1120.
Pardridge, W. M. (1986). Receptor-mediated peptide transport through the blood-brain barrier. Endocrine Reviews, 7, 314–330.
Pardridge, W. M. (1994). New approaches to drug delivery through the blood-brain barrier. Trends in Biotechnology, 12, 239–245.
Pardridge, W. M. (2001). Crossing the blood-brain barrier: Are we getting it right? Drug Discovery Today, 6, 1–2.
Pardridge, W. M. (2005). The blood-brain barrier: bottleneck in brain drug development. NeuroRx, 2, 3–14.
Pardridge, W. M. (2006). Molecular Trojan horses for blood-brain barrier drug delivery. Discovery Medicine, 6, 139–143.
Pardridge, W. M. (2007). Blood-brain barrier delivery. Drug Discovery Today, 12, 54–61.
Pardridge, W. M. (2010). Biologic TNFalpha-inhibitors that cross the human blood-brain barrier. Bioengineered Bugs, 1, 231–234.
Pardridge, W. M. (2012). Drug transport across the blood-brain barrier. Journal of Cerebral Blood Flow & Metabolism, 32, 1959–1972.
Pardridge, W. M., Kumagai, A. K., & Eisenberg, J. B. (1987). Chimeric peptides as a vehicle for peptide pharmaceutical delivery through the blood-brain barrier. Biochemical and Biophysical Research Communications, 146, 307–313.
Parenteau, J., Klinck, R., Good, L., Langel, Ü., Wellinger, R. J., & Elela, S. A. (2005). Free uptake of cell-penetrating peptides by fission yeast. FEBS Letters, 579, 4873–4878.
Park, D., Lee, J. Y., Cho, H. K., Hong, W. J., Kim, J., Seo, H., et al. (2018a). Cell-penetrating peptide-patchy deformable polymeric nanovehicles with enhanced cellular uptake and transdermal delivery. Biomacromolecules.
Park, J., Han, J. H., Myung, S. H., Seo, Y. W., & Kim, T. H. (2018b). MTD-like motif of a BH3-only protein, BNIP1, induces necrosis accompanied by an intracellular calcium spike. Biochemical and Biophysical Research Communications, 495, 1661–1667.
Patel, M. M., & Patel, B. M. (2017). Crossing the blood-brain barrier: Recent advances in drug delivery to the brain. CNS Drugs, 31, 109–133.
Patel, R. R., Sundin, G. W., Yang, C. H., Wang, J., Huntley, R. B., Yuan, X., et al. (2017). Exploration of using antisense Peptide Nucleic Acid (PNA)-cell Penetrating Peptide (CPP) as a novel bactericide against fire blight pathogen Erwinia amylovora. Frontiers in Microbiology, 8, 687.
Patra, S., Roy, E., Madhuri, R., & Sharma, P. K. (2016). The next generation cell-penetrating peptide and carbon dot conjugated nano-liposome for transdermal delivery of curcumin. Biomaterials Science, 4, 418–429.
Peng, J., Rao, Y., Yang, X., Jia, J., Wu, Y., Lu, J., et al. (2017). Targeting neuronal nitric oxide synthase by a cell penetrating peptide Tat-LK15/siRNA bioconjugate. Neuroscience Letters, 650, 153–160.
Pepper, J. T., Maheshwari, P., & Eudes, F. (2017a). Adsorption of cell-penetrating peptide Tat2 and polycation luviquat FC-370 to triticale microspore exine. Colloids and Surfaces B: Biointerfaces, 157, 207–214.
Pepper, J. T., Maheshwari, P., Ziemienowicz, A., Hazendonk, P., Kovalchuk, I., & Eudes, F. (2017b). Tetrabutylphosphonium bromide reduces size and polydispersity index of Tat2:siRNA nano-complexes for triticale RNAi. Frontiers in Molecular Biosciences, 4, 30.
Perera, Y., Costales, H. C., Diaz, Y., Reyes, O., Farina, H. G., Mendez, L., et al. (2012). Sensitivity of tumor cells towards CIGB-300 anticancer peptide relies on its nucleolar localization. Journal of Peptide Science, 18, 215–223.
Pero, S. C., Shukla, G. S., Cookson, M. M., Flemer, S., Jr., & Krag, D. N. (2007). Combination treatment with Grb7 peptide and Doxorubicin or Trastuzumab (Herceptin) results in cooperative cell growth inhibition in breast cancer cells. British Journal of Cancer, 96, 1520–1525.
Petrescu, A. D., Vespa, A., Huang, H., McIntosh, A. L., Schroeder, F., & Kier, A. B. (2009). Fluorescent sterols monitor cell penetrating peptide Pep-1 mediated uptake and intracellular targeting of cargo protein in living cells. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1788, 425–441.
Petrilli, R., Eloy, J. O., Praca, F. S., del Ciampo, J. O., Fantini, M. A., Fonseca, M. J., et al. (2016). Liquid crystalline nanodispersions functionalized with cell-penetrating peptides for topical delivery of short-interfering RNAs: A proposal for silencing a pro-inflammatory cytokine in cutaneous diseases. Journal of Biomedical Nanotechnology, 12, 1063–1075.
Poduslo, J. F., & Curran, G. L. (1994). Glycation increases the permeability of proteins across the blood-nerve and blood-brain barriers. Molecular Brain Research, 23, 157–162.
Ponnappan, N., Budagavi, D. P., & Chugh, A. (2017). CyLoP-1: Membrane-active peptide with cell-penetrating and antimicrobial properties. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1859, 167–176.
Pooga, M., Hällbrink, M., Zorko, M., & Langel, Ü. (1998). Cell penetration by transportan. The FASEB Journal, 12, 67–77.
Pouniotis, D., Tang, C. K., Apostolopoulos, V., & Pietersz, G. (2016). Vaccine delivery by penetratin: Mechanism of antigen presentation by dendritic cells. Immunologic Research, 64, 887–900.
Puckett, C. A., & Barton, J. K. (2010). Targeting a ruthenium complex to the nucleus with short peptides. Bioorganic & Medicinal Chemistry, 18, 3564–3569.
Puria, R., Sahi, S., & Nain, V. (2012). HER2+ breast cancer therapy: By CPP-ZFN mediated targeting of mTOR? Technology in Cancer Research & Treatment, 11, 175–180.
Qi, X., Droste, T., & Kao, C. C. (2011). Cell-penetrating peptides derived from viral capsid proteins. Molecular Plant-Microbe Interactions, 24, 25–36.
Qian, Z. M., Li, H., Sun, H., & Ho, K. (2002). Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway. Pharmacological Reviews, 54, 561–587.
Qifan, W., Fen, N., Ying, X., Xinwei, F., Jun, D., & Ge, Z. (2016). iRGD-targeted delivery of a pro-apoptotic peptide activated by cathepsin B inhibits tumor growth and metastasis in mice. Tumor Biology, 11, 11.
Raagel, H., Lust, M., Uri, A., & Pooga, M. (2008). Adenosine-oligoarginine conjugate, a novel bisubstrate inhibitor, effectively dissociates the actin cytoskeleton. The FEBS Journal, 275, 3608–3624.
Radis-Baptista, G., de la Torre, B. G., & Andreu, D. (2008). A novel cell-penetrating peptide sequence derived by structural minimization of a snake toxin exhibits preferential nucleolar localization. Journal of Medicinal Chemistry, 51, 7041–7044.
Radis-Baptista, G., de la Torre, B. G., & Andreu, D. (2012). Insights into the uptake mechanism of NrTP, a cell-penetrating peptide preferentially targeting the nucleolus of tumour cells. Chemical Biology & Drug Design, 79, 907–915.
Radis-Baptista, G., & Kerkis, I. (2011). Crotamine, a small basic polypeptide myotoxin from rattlesnake venom with cell-penetrating properties. Current Pharmaceutical Design, 17, 4351–4361.
Ran, R., Wang, H., Liu, Y., Hui, Y., Sun, Q., & Seth, A., et al. (2018). Microfluidic self-assembly of a combinatorial library of single- and dual-ligand liposomes for in vitro and in vivo tumor targeting. European Journal of Pharmaceutics and Biopharmaceutics.
Ran, Y., Liang, Z., & Gao, C. (2017). Current and future editing reagent delivery systems for plant genome editing. Science China Life Sciences, 60, 490–505.
Rao, K. S., Reddy, M. K., Horning, J. L., & Labhasetwar, V. (2008). TAT-conjugated nanoparticles for the CNS delivery of anti-HIV drugs. Biomaterials, 29, 4429–4438.
Rassu, G., Soddu, E., Posadino, A. M., Pintus, G., Sarmento, B., Giunchedi, P., et al. (2017). Nose-to-brain delivery of BACE1 siRNA loaded in solid lipid nanoparticles for Alzheimer’s therapy. Colloids and Surfaces B: Biointerfaces, 152, 296–301.
Regberg, J., Vasconcelos, L., Madani, F., Langel, Ü., & Hällbrink, M. (2016). pH-responsive PepFect cell-penetrating peptides. International Journal of Pharmaceutics, 501, 32–38.
Ren, J., Shen, S., Wang, D., Xi, Z., Guo, L., Pang, Z., et al. (2012a). The targeted delivery of anticancer drugs to brain glioma by PEGylated oxidized multi-walled carbon nanotubes modified with angiopep-2. Biomaterials, 33, 3324–3333.
Ren, Y., Cheung, H. W., Von Maltzhan, G., Agrawal, A., Cowley, G. S., Weir, B. A., et al. (2012b). Targeted tumor-penetrating siRNA nanocomplexes for credentialing the ovarian cancer oncogene ID4. Science Translational Medicine, 4, 147ra112.
Resina, S., Abes, S., Turner, J. J., Prevot, P., Travo, A., Clair, P., et al. (2007). Lipoplex and peptide-based strategies for the delivery of steric-block oligonucleotides. International Journal of Pharmaceutics, 344, 96–102.
Rhee, M., & Davis, P. (2006). Mechanism of uptake of C105Y, a novel cell-penetrating peptide. Journal of Biological Chemistry, 281, 1233–1240.
Richardson, A., Muir, L., Mousdell, S., Sexton, D., Jones, S., Howl, J., et al. (2018). Modulation of mitochondrial activity in HaCaT keratinocytes by the cell penetrating peptide Z-Gly-RGD(DPhe)-mitoparan. BMC Research Notes, 11, 82.
Rip, J., Schenk, G. J., & de Boer, A. G. (2009). Differential receptor-mediated drug targeting to the diseased brain. Expert Opinion on Drug Delivery, 6, 227–237.
Robbins, J., Dilworth, S. M., Laskey, R. A., & Dingwall, C. (1991). Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell, 64, 615–623.
Rodrigues, M., Andreu, D., & Santos, N. C. (2015). Uptake and cellular distribution of nucleolar targeting peptides (NrTPs) in different cell types. Biopolymers, 104, 101–109.
Rodriguez-Moreno, L., Song, Y., & Thomma, B. P. (2017). Transfer and engineering of immune receptors to improve recognition capacities in crops. Current Opinion in Plant Biology, 38, 42–49.
Rogers, F. A., Manoharan, M., Rabinovitch, P., Ward, D. C., & Glazer, P. M. (2004). Peptide conjugates for chromosomal gene targeting by triplex-forming oligonucleotides. Nucleic Acids Research, 32, 6595–6604.
Rosenbluh, J., Singh, S. K., Gafni, Y., Graessmann, A., & Loyter, A. (2004). Non-endocytic penetration of core histones into petunia protoplasts and cultured cells: A novel mechanism for the introduction of macromolecules into plant cells. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1664, 230–240.
Ross, M. F., Filipovska, A., Smith, R. A., Gait, M. J., & Murphy, M. P. (2004). Cell-penetrating peptides do not cross mitochondrial membranes even when conjugated to a lipophilic cation: Evidence against direct passage through phospholipid bilayers. Biochemical Journal, 383, 457–468.
Rothbard, J. B., Garlington, S., Lin, Q., Kirschberg, T., Kreider, E., McGrane, P. L., et al. (2000). Conjugation of arginine oligomers to cyclosporin A facilitates topical delivery and inhibition of inflammation. Nature Medicine, 6, 1253–1257.
Roy, R. N., Lomakin, I. B., Gagnon, M. G., & Steitz, T. A. (2015). The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nature Structural & Molecular Biology, 22, 466–469.
Ruan, S., Yuan, M., Zhang, L., Hu, G., Chen, J., Cun, X., et al. (2015). Tumor microenvironment sensitive doxorubicin delivery and release to glioma using angiopep-2 decorated gold nanoparticles. Biomaterials, 37, 425–435.
Ruge, C. A., Kirch, J., & Lehr, C. M. (2013). Pulmonary drug delivery: From generating aerosols to overcoming biological barriers-therapeutic possibilities and technological challenges. The Lancet Respiratory Medicine, 1, 402–413.
Ruoslahti, E. (2017). Tumor penetrating peptides for improved drug delivery. Advanced Drug Delivery Reviews, 111, 3–12.
Räägel, H., Säälik, P., Langel, Ü., & Pooga, M. (2011). Mapping of protein transduction pathways with fluorescent microscopy. Methods Mol Biol, 683, 165–179.
Sakhrani, N. M., & Padh, H. (2013). Organelle targeting: third level of drug targeting. Drug Design, Development and Therapy, 7, 585–599.
Sakurai, Y., Mizumura, W., Murata, M., Hada, T., Yamamoto, S., Ito, K., et al. (2017). Efficient siRNA delivery by lipid nanoparticles modified with a non-standard macrocyclic peptide for EpCAM-targeting. Molecular Pharmaceutics, 8.
Sallevelt, S. C., De Die-Smulders, C. E., Hendrickx, A. T., Hellebrekers, D. M., de Coo, I. F., Alston, C. L., et al. (2017). De novo mtDNA point mutations are common and have a low recurrence risk. Journal of Medical Genetics, 54, 73–83.
Samuel, J. P., Samboju, N. C., Yau, K. Y., Lin, G., Webb, S. R., & Burroughs, F. (2013). Quantum dot carrier peptide conjugates suitable for imaging and delivery applications in plants. Google Patents.
Santra, S., Yang, H., Stanley, J. T., Holloway, P. H., Moudgil, B. M., Walter, G., et al. (2005). Rapid and effective labeling of brain tissue using TAT-conjugated CdS:Mn/ZnS quantum dots. Chemical Communications (Camb), 3144–3146.
Sato, Y., Nakamura, T., Yamada, Y., Akita, H., & Harashima, H. (2014). Multifunctional enveloped nanodevices (MENDs). Advances in Genetics, 88, 139–204.
Sawahel, W. A. (2001). Stable genetic transformation of cotton plants using polybrene-spermidine treatment. Plant Molecular Biology Reporter, 19, 377.
Savariar, E. N., Felsen, C. N., Nashi, N., Jiang, T., Ellies, L. G., Steinbach, P., et al. (2013). Real-time in vivo molecular detection of primary tumors and metastases with ratiometric activatable cell-penetrating peptides. Cancer Research, 73, 855–864.
Schulz, R., Yamamoto, K., Klossek, A., Flesch, R., Honzke, S., Rancan, F., et al. (2017). Data-based modeling of drug penetration relates human skin barrier function to the interplay of diffusivity and free-energy profiles. Proceedings of the National Academy of Sciences USA, 114, 3631–3636.
Schwarze, S. R., Ho, A., Vocero-Akbani, A., & Dowdy, S. F. (1999). In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science, 285, 1569–1572.
Selmin, F., Magri, G., Gennari, C. G., Marchiano, S., Ferri, N., & Pellegrino, S. (2017). Development of poly(lactide-co-glycolide) nanoparticles functionalized with a mitochondria penetrating peptide. Journal of Peptide Science, 23, 182–188.
Shabanpoor, F., Hammond, S. M., Abendroth, F., Hazell, G., Wood, M. J. A., & Gait, M. J. (2017). Identification of a peptide for systemic brain delivery of a morpholino oligonucleotide in mouse models of spinal muscular atrophy. Nucleic Acid Therapeutics, 27, 130–143.
Shamay, Y., Shpirt, L., Ashkenasy, G., & David, A. (2014). Complexation of cell-penetrating peptide-polymer conjugates with polyanions controls cells uptake of HPMA copolymers and anti-tumor activity. Pharmaceutical Research, 31, 768–779.
Sharma, G., Modgil, A., Zhong, T., Sun, C., & Singh, J. (2014). Influence of short-chain cell-penetrating peptides on transport of doxorubicin encapsulating receptor-targeted liposomes across brain endothelial barrier. Pharmaceutical Research, 31, 1194–1209.
Shearer, A. M., Rana, R., Austin, K., Baleja, J. D., Nguyen, N., Bohm, A., et al. (2016). Targeting liver fibrosis with a cell-penetrating Protease-activated Receptor-2 (PAR2) pepducin. Journal of Biological Chemistry, 291, 23188–23198.
Shenoy, N., Kessel, R., Bhagat, T. D., Bhattacharyya, S., Yu, Y., McMahon, C., et al. (2012). Alterations in the ribosomal machinery in cancer and hematologic disorders. Journal of Hematology & Oncology, 5, 1756–8722.
Shi, K., Long, Y., Xu, C., Wang, Y., Qiu, Y., Yu, Q., et al. (2015). Liposomes combined an integrin alphabeta-specific vector with pH-responsible cell-penetrating property for highly effective antiglioma therapy through the blood-brain barrier. ACS Applied Materials & Interfaces.
Shi, N. Q., Gao, W., Xiang, B., & Qi, X. R. (2012). Enhancing cellular uptake of activable cell-penetrating peptide-doxorubicin conjugate by enzymatic cleavage. International Journal of Nanomedicine, 7, 1613–1621.
Shi, N. Q., Qi, X. R., Xiang, B., & Zhang, Y. (2014). A survey on “Trojan Horse” peptides: Opportunities, issues and controlled entry to “Troy”. Journal of Controlled Release, 194, 53–70.
Shim, Y.-S., Eudes, F., & Kovalchuk, I. (2013). dsDNA and protein co-delivery in triticale microspores. Vitro Cellular & Developmental Biology - Plant, 49, 156–165.
Shin, M. C., Zhang, J., Min, K. A., Lee, K., Moon, C., Balthasar, J. P., et al. (2014a). Combination of antibody targeting and PTD-mediated intracellular toxin delivery for colorectal cancer therapy. Journal of Controlled Release, 194, 197–210.
Shin, T. H., Sung, E. S., Kim, Y. J., Kim, K. S., Kim, S. H., Kim, S. K., et al. (2014b). Enhancement of the tumor penetration of monoclonal antibody by fusion of a neuropilin-targeting peptide improves the antitumor efficacy. Molecular Cancer Therapeutics, 13, 651–661.
Shteinfer-Kuzmine, A., Arif, T., Krelin, Y., Tripathi, S. S., Paul, A., & Shoshan-Barmatz, V. (2017). Mitochondrial VDAC1-based peptides: Attacking oncogenic properties in glioblastoma. Oncotarget, 8, 31329–31346.
Sibrian-Vazquez, M., Jensen, T. J., & Vicente, M. G. (2008). Synthesis, characterization, and metabolic stability of porphyrin-peptide conjugates bearing bifunctional signaling sequences. Journal of Medicinal Chemistry, 51, 2915–2923.
Simon, M. J., Kang, W. H., Gao, S., Banta, S., & Morrison, B., III. (2011). TAT is not capable of transcellular delivery across an intact endothelial monolayer in vitro. Annals of Biomedical Engineering, 39, 394–401.
Skarlatos, S., Yoshikawa, T., & Pardridge, W. M. (1995). Transport of [125I]transferrin through the rat blood-brain barrier. Brain Research, 683, 164–171.
Skrlj, N., & Dolinar, M. (2014). New engineered antibodies against prions. Bioengineered, 5, 10–14.
Skrlj, N., Drevensek, G., Hudoklin, S., Romih, R., Curin Serbec, V., & Dolinar, M. (2013). Recombinant single-chain antibody with the Trojan peptide penetratin positioned in the linker region enables cargo transfer across the blood-brain barrier. Applied Biochemistry and Biotechnology, 169, 159–169.
Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015). The voltage-dependent anion channel 1 mediates amyloid beta toxicity and represents a potential target for alzheimer disease therapy. Journal of Biological Chemistry, 290, 30670–30683.
Snyder, E. L., Meade, B. R., Saenz, C. C., & Dowdy, S. F. (2004). Treatment of terminal peritoneal carcinomatosis by a transducible p53-activating peptide. PLoS Biology, 2, 17.
Snyder, E. L., Saenz, C. C., Denicourt, C., Meade, B. R., Cui, X. S., Kaplan, I. M., et al. (2005). Enhanced targeting and killing of tumor cells expressing the CXC chemokine receptor 4 by transducible anticancer peptides. Cancer Research, 65, 10646–10650.
Solomon, M., & Muro, S. (2017). Lysosomal enzyme replacement therapies: Historical development, clinical outcomes, and future perspectives. Advanced Drug Delivery Reviews, 11, 30060–30061.
Song, H., Zhang, J., Wang, W., Huang, P., Zhang, Y., Liu, J., et al. (2015). Acid-responsive PEGylated doxorubicin prodrug nanoparticles for neuropilin-1 receptor-mediated targeted drug delivery. Colloids and Surfaces B: Biointerfaces, 136, 365–374.
Sosnowski, T. R. (2016). Selected engineering and physicochemical aspects of systemic drug delivery by inhalation. Current Pharmaceutical Design, 22, 2453–2462.
Sousa, F., Castro, P., Fonte, P., Kennedy, P. J., Neves-Petersen, M. T., & Sarmento, B. (2016). Nanoparticles for the delivery of therapeutic antibodies: Dogma or promising strategy? Expert Opinion on Drug Delivery, 29, 1–14.
Spencer, B., Williams, S., Rockenstein, E., Valera, E., Xin, W., Mante, M., et al. (2016). Alpha-synuclein conformational antibodies fused to penetratin are effective in models of Lewy body disease. Annals of Clinical and Translational Neurology, 3, 588–606.
Spencer, B. J., & Verma, I. M. (2007). Targeted delivery of proteins across the blood-brain barrier. Proceedings of the National Academy of Sciences USA, 104, 7594–7599.
Srimanee, A., Arvanitidou, M., Kim, K., Hallbrink, M., & Langel, U. (2018). Cell-penetrating peptides for siRNA delivery to glioblastomas. Peptides, 104, 62–69.
Srimanee, A., Regberg, J., Hallbrink, M., Vajragupta, O., & Langel, U. (2016). Role of scavenger receptors in peptide-based delivery of plasmid DNA across a blood-brain barrier model. International Journal of Pharmaceutics, 500, 128–135.
Srimanee, A., Regberg, J., Hällbrink, M., Kurrikoff, K., Veiman, K.-L., Vajragupta, O., et al. (2014). Peptide based delivery of oligonucleotides across blood-brain barrier model. Journal of Peptide Research and Therapeutics, 20, 169–178.
Stalmans, S., Bracke, N., Wynendaele, E., Gevaert, B., Peremans, K., Burvenich, C., et al. (2015). Cell-penetrating peptides selectively cross the blood-brain barrier in vivo. PLoS One, 10.
Suda, K., Murakami, T., Gotoh, N., Fukuda, R., Hashida, Y., Hashida, M., et al. (2017). High-density lipoprotein mutant eye drops for the treatment of posterior eye diseases. Journal of Controlled Release, 266, 301–309.
Sugahara, K. N., Teesalu, T., Karmali, P. P., Kotamraju, V. R., Agemy, L., Greenwald, D. R., et al. (2010). Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science, 328, 1031–1035.
Suk, J. S., Kim, A. J., Trehan, K., Schneider, C. S., Cebotaru, L., Woodward, O. M., et al. (2014). Lung gene therapy with highly compacted DNA nanoparticles that overcome the mucus barrier. Journal of Controlled Release, 178, 8–17.
Sumbria, R. K., Boado, R. J., & Pardridge, W. M. (2013). Combination stroke therapy in the mouse with blood-brain barrier penetrating IgG-GDNF and IgG-TNF decoy receptor fusion proteins. Brain Research, 24, 91–96.
Sun, L., Xie, S., Ji, X., Zhang, J., Wang, D., Lee, S. J., et al. (2018). MMP-2-responsive fluorescent nanoprobes for enhanced selectivity of tumor cell uptake and imaging. Biomaterials Science.
Sun, Y., Xian, L., Xing, H., Yu, J., Yang, Z., Yang, T., et al. (2016). Factors influencing the nuclear targeting ability of nuclear localization signals. Journal of Drug Targeting, 24, 927–933.
Suresh, A., & Kim, Y. C. (2013). Translocation of cell penetrating peptides on Chlamydomonas reinhardtii. Biotechnology and Bioengineering, 110, 2795–2801.
Swiecicki, J. M., di Pisa, M., Lippi, F., Chwetzoff, S., Mansuy, C., Trugnan, G., et al. (2015). Unsaturated acyl chains dramatically enhanced cellular uptake by direct translocation of a minimalist oligo-arginine lipopeptide. Chemical Communications (Camb), 51, 14656–14659.
Szeto, H. H. (2006a). Cell-permeable, mitochondrial-targeted, peptide antioxidants. The AAPS Journal, 8, E277–E283.
Szeto, H. H. (2006b). Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents. The AAPS Journal, 8, E521–E531.
Tacken, P. J., Joosten, B., Reddy, A., Wu, D., Eek, A., Laverman, P., et al. (2008). No advantage of cell-penetrating peptides over receptor-specific antibodies in targeting antigen to human dendritic cells for cross-presentation. The Journal of Immunology, 180, 7687–7696.
Takara, K., Hatakeyama, H., Kibria, G., Ohga, N., Hida, K., & Harashima, H. (2012). Size-controlled, dual-ligand modified liposomes that target the tumor vasculature show promise for use in drug-resistant cancer therapy. Journal of Controlled Release, 162, 225–232.
Taki, H., Kanazawa, T., Akiyama, F., Takashima, Y., & Okada, H. (2012). Intranasal delivery of camptothecin-loaded tat-modified nanomicells for treatment of intracranial brain tumors. Pharmaceuticals (Basel), 5, 1092–1102.
Talvensaari-Mattila, A., Paakko, P., & Turpeenniemi-Hujanen, T. (2003). Matrix metalloproteinase-2 (MMP-2) is associated with survival in breast carcinoma. British Journal of Cancer, 89, 1270–1275.
Tan, M., Lan, K. H., Yao, J., Lu, C. H., Sun, M., Neal, C. L., et al. (2006). Selective inhibition of ErbB2-overexpressing breast cancer in vivo by a novel TAT-based ErbB2-targeting signal transducers and activators of transcription 3-blocking peptide. Cancer Research, 66, 3764–3772.
Tan, R. S., Naruchi, K., Amano, M., Hinou, H., & Nishimura, S. (2015). Rapid endolysosomal escape and controlled intracellular trafficking of cell surface mimetic quantum-dots-anchored peptides and glycopeptides. ACS Chemical Biology, 10, 2073–2086.
Tashima, T. (2018). Effective cancer therapy based on selective drug delivery into cells across their membrane using receptor-mediated endocytosis. Bioorganic & Medicinal Chemistry Letters.
Taylor, B. N., Mehta, R. R., Yamada, T., Lekmine, F., Christov, K., Chakrabarty, A. M., et al. (2009). Noncationic peptides obtained from azurin preferentially enter cancer cells. Cancer Research, 69, 537–546.
Thomas, F. C., Taskar, K., Rudraraju, V., Goda, S., Thorsheim, H. R., Gaasch, J. A., et al. (2009). Uptake of ANG1005, a novel paclitaxel derivative, through the blood-brain barrier into brain and experimental brain metastases of breast cancer. Pharmaceutical Research, 26, 2486–2494.
Tkachenko, A. G., Xie, H., Coleman, D., Glomm, W., Ryan, J., Anderson, M. F., et al. (2003). Multifunctional gold nanoparticle-peptide complexes for nuclear targeting. Journal of the American Chemical Society, 125, 4700–4701.
Toba, M., Alzoubi, A., O’Neill, K., Abe, K., Urakami, T., Komatsu, M., et al. (2014). A novel vascular homing peptide strategy to selectively enhance pulmonary drug efficacy in pulmonary arterial hypertension. The American Journal of Pathology, 184, 369–375.
Torchilin, V. P. (2006). Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Annu Rev Biomed Eng, 8, 343–375.
Tünnemann, G., Martin, R. M., Haupt, S., Patsch, C., Edenhofer, F., & Cardoso, M. C. (2006). Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells. The FASEB Journal, 20, 1775–1784.
Uchida, T., Kanazawa, T., Takashima, Y., & Okada, H. (2011). Development of an efficient transdermal delivery system of small interfering RNA using functional peptides, Tat and AT-1002. Chemical and Pharmaceutical Bulletin (Tokyo), 59, 196–201.
Urgard, E., Lorents, A., Klaas, M., Padari, K., Viil, J., Runnel, T., et al. (2016). Pre-administration of PepFect6-microRNA-146a nanocomplexes inhibits inflammatory responses in keratinocytes and in a mouse model of irritant contact dermatitis. Journal of Controlled Release, 235, 195–204.
Wada, S. I., Iwata, M., Ozaki, Y., Ozaki, T., Hayashi, J., & Urata, H. (2016). Design of cyclic RGD-conjugated Aib-containing amphipathic helical peptides for targeted delivery of small interfering RNA. Bioorganic & Medicinal Chemistry, 24, 4478–4485.
Wadia, J. S., Stan, R. V., & Dowdy, S. F. (2004). Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nature Medicine, 10, 310–315.
Wagner, S., Zensi, A., Wien, S. L., Tschickardt, S. E., Maier, W., Vogel, T., et al. (2012). Uptake mechanism of ApoE-modified nanoparticles on brain capillary endothelial cells as a blood-brain barrier model. PLoS One, 7, 1.
Wagstaff, K. M., Glover, D. J., Tremethick, D. J., & Jans, D. A. (2007). Histone-mediated transduction as an efficient means for gene delivery. Molecular Therapy, 15, 721–731.
Wahlmuller, F. C., Yang, H., Furtmuller, M., & Geiger, M. (2017). Regulation of the extracellular SERPINA5 (Protein C Inhibitor) penetration through cellular membranes. Adv Exp Med Biol, 22.
Wallbrecher, R., Chene, P., Ruetz, S., Stachyra, T., Vorherr, T., & Brock, R. (2017). A critical assessment of the synthesis and biological activity of p53/human double minute 2-stapled peptide inhibitors. British Journal of Pharmacology, 174, 2613–2622.
Walther, R., Rautio, J., & Zelikin, A. N. (2017). Prodrugs in medicinal chemistry and enzyme prodrug therapies. Advanced Drug Delivery Reviews, 1, 30097-2.
van Duijnhoven, S. M., Robillard, M. S., Nicolay, K., & Grull, H. (2011). Tumor targeting of MMP-2/9 activatable cell-penetrating imaging probes is caused by tumor-independent activation. Journal of Nuclear Medicine, 52, 279–286.
van Duijnhoven, S. M., Robillard, M. S., Nicolay, K., & Grull, H. (2015). In vivo biodistribution of radiolabeled MMP-2/9 activatable cell-penetrating peptide probes in tumor-bearing mice. Contrast Media & Molecular Imaging, 10, 59–66.
van Lith, S. A. M., Van Den Brand, D., Wallbrecher, R., Wubbeke, L., van Duijnhoven, S. M. J., Makinen, P. I., et al. (2017). The effect of subcellular localization on the efficiency of EGFR-targeted VHH photosensitizer conjugates. European Journal of Pharmaceutics and Biopharmaceutics.
Wang, H. Y., Chen, J. X., Sun, Y. X., Deng, J. Z., Li, C., Zhang, X. Z., et al. (2011). Construction of cell penetrating peptide vectors with N-terminal stearylated nuclear localization signal for targeted delivery of DNA into the cell nuclei. Journal of Controlled Release, 155, 26–33.
Wang, L., Hao, Y., Li, H., Zhao, Y., Meng, D., Li, D., et al. (2015a). Co-delivery of doxorubicin and siRNA for glioma therapy by a brain targeting system: angiopep-2-modified poly(lactic-co-glycolic acid) nanoparticles. Journal of Drug Targeting, 1–15.
Wang, S., Huttmann, G., Zhang, Z., Vogel, A., Birngruber, R., Tangutoori, S., et al. (2015b). Light-controlled delivery of monoclonal antibodies for targeted photoinactivation of Ki-67. Molecular Pharmaceutics, 12, 3272–3281.
Wang, Z. Y., Liu, J. Y., Yang, C. B., Malampati, S., Huang, Y. Y., Li, M. X., et al. (2017). Neuroprotective natural products for the treatment of Parkinson’s disease by targeting the autophagy-lysosome pathway: A systematic review. Phytotherapy Research, 31, 1119–1127.
Watkins, G. A., Jones, E. F., Scott Shell, M., Vanbrocklin, H. F., Pan, M. H., Hanrahan, S. M., et al. (2009). Development of an optimized activatable MMP-14 targeted SPECT imaging probe. Bioorganic & Medicinal Chemistry, 17, 653–659.
Watson, V. G., Drake, K. M., Peng, Y., & Napper, A. D. (2013). Development of a high-throughput screening-compatible assay for the discovery of inhibitors of the AF4-AF9 interaction using AlphaScreen technology. Assay and Drug Development Technologies, 11, 253–268.
Vazquez, O., Blanco-Canosa, J. B., Vazquez, M. E., Martinez-Costas, J., Castedo, L., & Mascarenas, J. L. (2008). Efficient DNA binding and nuclear uptake by distamycin derivatives conjugated to octa-arginine sequences. Chembiochem, 9, 2822–2829.
Veiman, K. L., Kunnapuu, K., Lehto, T., Kiisholts, K., Pärn, K., Langel, Ü., et al. (2015). PEG shielded MMP sensitive CPPs for efficient and tumor specific gene delivery in vivo. Journal of Controlled Release, 209, 238–247.
Veiman, K. L., Mäger, I., Ezzat, K., Margus, H., Lehto, T., Langel, K., et al. (2013). PepFect14 peptide vector for efficient gene delivery in cell cultures. Molecular Pharmaceutics, 10, 199–210.
Weinstain, R., Savariar, E. N., Felsen, C. N., & Tsien, R. Y. (2014). In vivo targeting of hydrogen peroxide by activatable cell-penetrating peptides. Journal of the American Chemical Society, 136, 874–877.
Weisbart, R. H., Chan, G., Jordaan, G., Noble, P. W., Liu, Y., Glazer, P. M., et al. (2015). DNA-dependent targeting of cell nuclei by a lupus autoantibody. Scientific Reports, 5.
Weissig, V., & Torchilin, V. P. (2001). Cationic bolasomes with delocalized charge centers as mitochondria-specific DNA delivery systems. Advanced Drug Delivery Reviews, 49, 127–149.
Welch, J. J., Swanekamp, R. J., King, C., Dean, D. A., & Nilsson, B. L. (2016). Functional delivery of siRNA by disulfide-constrained cyclic amphipathic peptides. ACS Medicinal Chemistry Letters, 7, 584–589.
Venkatachalam, A., Wood, C., Hu, Q., & Alwayn, I. (2015). Delivery of Heme Oxygenase-1-Cell Penetrating Peptide (HO-1-CPP) into hepatocytes, Kupffer and Islet cells in in vitro and ex vivo models of cold ischemia. American Journal of Transplantation, 15.
Verheij, M. M., Vendruscolo, L. F., Caffino, L., Giannotti, G., Cazorla, M., Fumagalli, F., et al. (2016). Systemic delivery of a brain-penetrant TrkB antagonist reduces cocaine self-administration and normalizes TrkB signaling in the nucleus accumbens and prefrontal cortex. Journal of Neuroscience, 36, 8149–8159.
Whitney, M., Crisp, J. L., Olson, E. S., Aguilera, T. A., Gross, L. A., Ellies, L. G., et al. (2010). Parallel in vivo and in vitro selection using phage display identifies protease-dependent tumor-targeting peptides. Journal of Biological Chemistry, 285, 22532–22541.
Whitney, M., Savariar, E. N., Friedman, B., Levin, R. A., Crisp, J. L., Glasgow, H. L., et al. (2013). Ratiometric activatable cell-penetrating peptides provide rapid in vivo readout of thrombin activation. Angewandte Chemie International Edition, 52, 325–330.
Viht, K., Padari, K., Raidaru, G., Subbi, J., Tammiste, I., Pooga, M., et al. (2003). Liquid-phase synthesis of a pegylated adenosine-oligoarginine conjugate, cell-permeable inhibitor of cAMP-dependent protein kinase. Bioorganic & Medicinal Chemistry Letters, 13, 3035–3039.
Vij, M., Alam, S., Gupta, N., Gotherwal, V., Gautam, H., Ansari, K. M., et al. (2017). Non-invasive oil-based method to increase topical delivery of nucleic acids to skin. Molecular Therapy, 25, 1342–1352.
Vij, M., Natarajan, P., Pattnaik, B. R., Alam, S., Gupta, N., Santhiya, D., et al. (2016a). Non-invasive topical delivery of plasmid DNA to the skin using a peptide carrier. Journal of Controlled Release, 222, 159–168.
Vij, M., Natarajan, P., Yadav, A. K., Patil, K. M., Pandey, T., Gupta, N., et al. (2016b). Efficient cellular entry of (r-x-r)-type carbamate-plasmid DNA complexes and its implication for noninvasive topical DNA delivery to skin. Molecular Pharmaceutics, 13, 1779–1790.
Wlodkowic, D., Skommer, J., McGuinness, D., Hillier, C., & Darzynkiewicz, Z. (2009). ER-Golgi network–a future target for anti-cancer therapy. Leukemia Research, 33, 1440–1447.
Woldetsadik, A. D., Vogel, M. C., Rabeh, W. M., & Magzoub, M. (2017). Hexokinase II-derived cell-penetrating peptide targets mitochondria and triggers apoptosis in cancer cells. The FASEB Journal, 9.
Wonder, E., Simon-Gracia, L., Scodeller, P., Majzoub, R. N., Kotamraju, V. R., Ewert, K. K., et al. (2018). Competition of charge-mediated and specific binding by peptide-tagged cationic liposome-DNA nanoparticles in vitro and in vivo. Biomaterials, 166, 52–63.
Wu, J., Han, H., Jin, Q., Li, Z., Li, H., & Ji, J. (2017). Design and proof of programmed 5-Aminolevulinic acid prodrug nanocarriers for targeted photodynamic cancer therapy. ACS Applied Materials & Interfaces, 9, 14596–14605.
Wu, J., Zheng, Y., Liu, M., Shan, W., Zhang, Z., & Huang, Y. (2018). Biomimetic viruslike and charge reversible nanoparticles to sequentially overcome mucus and epithelial barriers for oral insulin delivery. ACS Applied Materials & Interfaces, 10, 9916–9928.
Wyatt, L. C., Moshnikova, A., Crawford, T., Engelman, D. M., Andreev, O. A., & Reshetnyak, Y. K. (2018). Peptides of pHLIP family for targeted intracellular and extracellular delivery of cargo molecules to tumors. Proceedings of the National Academy of Sciences USA, 115, E2811–E2818.
Xia, H., Gao, X., Gu, G., Liu, Z., Hu, Q., Tu, Y., et al. (2012). Penetratin-functionalized PEG-PLA nanoparticles for brain drug delivery. International Journal of Pharmaceutics, 436, 840–850.
Xia, H., Gao, X., Gu, G., Liu, Z., Zeng, N., Hu, Q., et al. (2011). Low molecular weight protamine-functionalized nanoparticles for drug delivery to the brain after intranasal administration. Biomaterials, 32, 9888–9898.
Xiang, B., Dong, D. W., Shi, N. Q., Gao, W., Yang, Z. Z., Cui, Y., et al. (2013). PSA-responsive and PSMA-mediated multifunctional liposomes for targeted therapy of prostate cancer. Biomaterials, 34, 6976–6991.
Xin, H., Sha, X., Jiang, X., Zhang, W., Chen, L., & Fang, X. (2012). Anti-glioblastoma efficacy and safety of paclitaxel-loading Angiopep-conjugated dual targeting PEG-PCL nanoparticles. Biomaterials, 33, 8167–8176.
Yaghini, E., Dondi, R., Tewari, K. M., Loizidou, M., Eggleston, I. M., & Macrobert, A. J. (2017). Endolysosomal targeting of a clinical chlorin photosensitiser for light-triggered delivery of nano-sized medicines. Scientific Reports, 7, 6059.
Yamada, Y., Furukawa, R., & Harashima, H. (2016). A dual-ligand liposomal system composed of a cell-penetrating peptide and a mitochondrial RNA aptamer synergistically facilitates cellular uptake and mitochondrial targeting. Journal of Pharmaceutical Sciences, 4, 00402.
Yamada, Y., Perez, S. M., Tabata, M., Abe, J., Yasuzaki, Y., & Harashima, H. (2015). Efficient and high-speed transduction of an antibody into living cells using a multifunctional nanocarrier system to control intracellular trafficking. Journal of Pharmaceutical Sciences, 104, 2845–2854.
Yamamoto, S., Kato, A., Sakurai, Y., Hada, T., & Harashima, H. (2017). Modality of tumor endothelial VEGFR2 silencing-mediated improvement in intratumoral distribution of lipid nanoparticles. Journal of Controlled Release, 251, 1–10.
Yameen, B., Choi, W. I., Vilos, C., Swami, A., Shi, J., & Farokhzad, O. C. (2014). Insight into nanoparticle cellular uptake and intracellular targeting. Journal of Controlled Release, 190, 485–499.
Yan, H., Wang, J., Yi, P., Lei, H., Zhan, C., Xie, C., et al. (2011). Imaging brain tumor by dendrimer-based optical/paramagnetic nanoprobe across the blood-brain barrier. Chemical Communications, 47, 8130–8132.
Yanez, R. J. R., Lamprecht, R., Granadillo, M., Torrens, I., Arcalis, E., Stoger, E., et al. (2017a). LALF32-51 -E7, a HPV-16 therapeutic vaccine candidate, forms protein body-like structures when expressed in Nicotiana benthamiana leaves. Plant Biotechnology Journal.
Yanez, R. J. R., Lamprecht, R., Granadillo, M., Weber, B., Torrens, I., Rybicki, E. P., et al. (2017b). Expression optimization of a cell membrane-penetrating human papillomavirus type 16 therapeutic vaccine candidate in Nicotiana benthamiana. PLoS One, 12, e0183177.
Yang, J., Li, Q., Yang, X., Feng, Y., Ren, X., Shi, C., et al. (2016). Multitargeting gene delivery systems for enhancing the transfection of endothelial cells. Macromolecular Rapid Communications, 37, 1926–1931.
Yang, Y., Xie, X., Cai, X., Wang, Z., Gong, W., Zhang, H., et al. (2015). A near-infrared two-photon-sensitive peptide-mediated liposomal delivery system. Colloids and Surfaces B: Biointerfaces, 128, 427–438.
Yang, Z. Z., Li, J. Q., Wang, Z. Z., Dong, D. W., & Qi, X. R. (2014). Tumor-targeting dual peptides-modified cationic liposomes for delivery of siRNA and docetaxel to gliomas. Biomaterials, 35, 5226–5239.
Ye, J., Shin, M. C., Liang, Q., He, H., & Yang, V. C. (2015). 15 years of ATTEMPTS: A macromolecular drug delivery system based on the CPP-mediated intracellular drug delivery and antibody targeting. Journal of Controlled Release, 205, 58–69.
Yoneda, Y., Semba, T., Kaneda, Y., Noble, R. L., Matsuoka, Y., Kurihara, T., et al. (1992). A long synthetic peptide containing a nuclear localization signal and its flanking sequences of SV40 T-antigen directs the transport of IgM into the nucleus efficiently. Experimental Cell Research, 201, 313–320.
Yoneda, Y., Steiniger, S. C., Capkova, K., Mee, J. M., Liu, Y., Kaufmann, G. F., et al. (2008). A cell-penetrating peptidic GRP78 ligand for tumor cell-specific prodrug therapy. Bioorganic & Medicinal Chemistry Letters, 18, 1632–1636.
Youn, P., Chen, Y., & Furgeson, D. Y. (2014). A myristoylated cell-penetrating peptide bearing a transferrin receptor-targeting sequence for neuro-targeted siRNA delivery. Molecular Pharmaceutics, 11, 486–495.
Younis, A., Siddique, M. I., Kim, C. K., & Lim, K. B. (2014). RNA Interference (RNAi) induced gene silencing: A promising approach of hi-tech plant breeding. International Journal of Biological Sciences, 10, 1150–1158.
Yu, Y. J., Zhang, Y., Kenrick, M., Hoyte, K., Luk, W., Lu, Y., et al. (2011). Boosting brain uptake of a therapeutic antibody by reducing its affinity for a transcytosis target. Science Translational Medicine, 3, 3002230.
Yuan, X., Lin, X., Manorek, G., & Howell, S. B. (2011). Challenges associated with the targeted delivery of gelonin to claudin-expressing cancer cells with the use of activatable cell penetrating peptides to enhance potency. BMC Cancer, 11, 1471–2407.
Yurlova, L., Derks, M., Buchfellner, A., Hickson, I., Janssen, M., Morrison, D., et al. (2014). The fluorescent two-hybrid assay to screen for protein-protein interaction inhibitors in live cells: targeting the interaction of p53 with Mdm2 and Mdm4. Journal of Biomolecular Screening, 19, 516–525.
Zannikou, M., Bellou, S., Eliades, P., Hatzioannou, A., Mantzaris, M. D., Carayanniotis, G., et al. (2016). DNA-histone complexes as ligands amplify cell penetration and nuclear targeting of anti-DNA antibodies via energy-independent mechanisms. Immunology, 147, 73–81.
Zaro, J. L., Vekich, J. E., Tran, T., & Shen, W. C. (2009). Nuclear localization of cell-penetrating peptides is dependent on endocytosis rather than cytosolic delivery in CHO cells. Molecular Pharmaceutics, 6, 337–344.
Zhan, C., Li, B., Hu, L., Wei, X., Feng, L., Fu, W., et al. (2011). Micelle-based brain-targeted drug delivery enabled by a nicotine acetylcholine receptor ligand. Angewandte Chemie International Edition, 50, 5482–5485.
Zhan, C., Yan, Z., Xie, C., & Lu, W. (2010). Loop 2 of Ophiophagus hannah toxin b binds with neuronal nicotinic acetylcholine receptors and enhances intracranial drug delivery. Molecular Pharmaceutics, 7, 1940–1947.
Zhang, Q., Tang, J., Fu, L., Ran, R., Liu, Y., Yuan, M., et al. (2013). A pH-responsive alpha-helical cell penetrating peptide-mediated liposomal delivery system. Biomaterials, 34, 7980–7993.
Zhang, T., Qu, H., Li, X., Zhao, B., Zhou, J., Li, Q., et al. (2010). Transmembrane delivery and biological effect of human growth hormone via a phage displayed peptide in vivo and in vitro. Journal of Pharmaceutical Science, 99, 4880–4891.
Zhao, B. Q., Guo, Y. R., Li, X. L., Zang, T., Qu, H. Y., Zhou, J. P., et al. (2011). Amelioration of dementia induced by Abeta 22-35 through rectal delivery of undecapeptide-hEGF to mouse brain. International Journal of Pharmaceutics, 405, 1–8.
Zhao, B. X., Zhao, Y., Huang, Y., Luo, L. M., Song, P., Wang, X., et al. (2012). The efficiency of tumor-specific pH-responsive peptide-modified polymeric micelles containing paclitaxel. Biomaterials, 33, 2508–2520.
Zhao, K., Luo, G., Giannelli, S., & Szeto, H. H. (2005). Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines. Biochemical Pharmacology, 70, 1796–1806.
Zhao, K., Luo, G., Zhao, G. M., Schiller, P. W., & Szeto, H. H. (2003). Transcellular transport of a highly polar 3+ net charge opioid tetrapeptide. Journal of Pharmacology and Experimental Therapeutics, 304, 425–432.
Zhao, X., Shang, T., Zhang, X., Ye, T., Wang, D., & Rei, L. (2016). Passage of Magnetic Tat-Conjugated Fe3O4@SiO2 nanoparticles across in vitro blood-brain barrier. Nanoscale Research Letters, 11, 451.
Zhao, Y., Lou, D., Burkett, J., & Kohler, H. (2001). Chemical engineering of cell penetrating antibodies. Journal of Immunological Methods, 254, 137–145.
Zhou, Q. H., Hui, E. K., Lu, J. Z., Boado, R. J., & Pardridge, W. M. (2011a). Brain penetrating IgG-erythropoietin fusion protein is neuroprotective following intravenous treatment in Parkinson’s disease in the mouse. Brain Research, 25, 315–320.
Zhou, Q. H., Lu, J. Z., Hui, E. K., Boado, R. J., & Pardridge, W. M. (2011b). Delivery of a peptide radiopharmaceutical to brain with an IgG-avidin fusion protein. Bioconjugate Chemistry, 22, 1611–1618.
Zhu, L., Kate, P., & Torchilin, V. P. (2012). Matrix metalloprotease 2-responsive multifunctional liposomal nanocarrier for enhanced tumor targeting. ACS Nano, 6, 3491–3498.
Zhu, L., Wang, T., Perche, F., Taigind, A., & Torchilin, V. P. (2013). Enhanced anticancer activity of nanopreparation containing an MMP2-sensitive PEG-drug conjugate and cell-penetrating moiety. Proceedings of the National Academy of Sciences USA, 110, 17047–17052.
Ziemienowicz, A., Pepper, J., & Eudes, F. (2015). Applications of CPPs in genome modulation of plants. Methods Mol Biol, 1324, 417–434.
Ziemienowicz, A., Shim, Y. S., Matsuoka, A., Eudes, F., & Kovalchuk, I. (2012). A novel method of transgene delivery into triticale plants using the Agrobacterium transferred DNA-derived nano-complex. Plant Physiology, 158, 1503–1513.
Zonin, E., Moscatiello, R., Miuzzo, M., Cavallarin, N., di Paolo, M. L., Sandona, D., et al. (2011). TAT-mediated aequorin transduction: An alternative approach for effective calcium measurements in plant cells. Plant and Cell Physiology, 52, 2225–2235.
Zou, Z., Sun, Z., Li, P., Feng, T., & Wu, S. (2016). Cre fused with RVG peptide mediates targeted genome editing in mouse brain cells in vivo. International Journal of Molecular Sciences, 17.
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Langel, Ü. (2019). Targeting Strategies. In: CPP, Cell-Penetrating Peptides. Springer, Singapore. https://doi.org/10.1007/978-981-13-8747-0_5
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