Abstract
This chapter will summarize the methods for functionalization used in CPP research. Due to the very wide field of CPP applications as well as the involvement of CPPs in multiple biochemical pathways, the methods are also multiple. Basically, most of the methods of chemistry, biophysics, biochemistry, cell signaling , molecular biology, imaging etc., has been used to understand the action of CPPs. Hence, here we try to describe briefly the most widely used methods with highest impact for CPP research. It seems that it is reasonable to classify the CPP methods into non-functional and functional, based on the raised questions when applied.
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Abbate, V., Reelfs, O., Hider, R. C., & Pourzand, C. (2015). Design of novel fluorescent mitochondria-targeted peptides with iron-selective sensing activity. Biochemical Journal, 469, 357–366.
Abes, S., Moulton, H. M., Clair, P., Prevot, P., Youngblood, D. S., Wu, R. P., et al. (2006). Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents. Journal of Controlled Release, 116, 304–313.
Abes, S., Moulton, H., Turner, J., Clair, P., Richard, J. P., Iversen, P., et al. (2007). Peptide-based delivery of nucleic acids: Design, mechanism of uptake and applications to splice-correcting oligonucleotides. Biochemical Society Transactions, 35, 53–55.
Abushahba, M. F., Mohammad, H., & Seleem, M. N. (2016). Targeting Multidrug-resistant Staphylococci with an anti-rpoA peptide nucleic acid conjugated to the HIV-1 TAT Cell Penetrating Peptide. Molecular Therapy—Nucleic Acids, 5, e339.
Afsari, H. S., Cardoso dos Santos, M., Linden, S., Chen, T., Qiu, X., Van Bergen En Henegouwen, et al. (2016). Time-gated FRET nanoassemblies for rapid and sensitive intra- and extracellular fluorescence imaging. Science Advances 2, e1600265.
Aksoy, I., Jauch, R., Eras, V., Chng, W. B., Chen, J., Divakar, U., et al. (2013). Sox transcription factors require selective interactions with Oct4 and specific transactivation functions to mediate reprogramming. Stem Cells, 31, 2632–2646.
Alberici, L., Roth, L., Sugahara, K. N., Agemy, L., Kotamraju, V. R., Teesalu, T., et al. (2013). De novo design of a tumor-penetrating peptide. Cancer Research, 73, 804–812.
Aldrian, G., Vaissiere, A., Konate, K., Seisel, Q., Vives, E., Fernandez, F., et al. (2017). PEGylation rate influences peptide-based nanoparticles mediated siRNA delivery in vitro and in vivo. Journal of Controlled Release, 256, 79–91.
Aldrian-Herrada, G., Desarmenien, M. G., Orcel, H., Boissin-Agasse, L., Mery, J., Brugidou, J., et al. (1998). A peptide nucleic acid (PNA) is more rapidly internalized in cultured neurons when coupled to a retro-inverso delivery peptide. The antisense activity depresses the target mRNA and protein in magnocellular oxytocin neurons. Nucleic Acids Research, 26, 4910–4916.
Allinquant, B., Hantraye, P., Mailleux, P., Moya, K., Bouillot, C., & Prochiantz, A. (1995). Downregulation of amyloid precursor protein inhibits neurite outgrowth in vitro. Journal of Cell Biology, 128, 919–927.
Alvarez, M. J., Subramaniam, P. S., Tang, L. H., Grunn, A., Aburi, M., Rieckhof, G., et al. (2018). A precision oncology approach to the pharmacological targeting of mechanistic dependencies in neuroendocrine tumors. Nature Genetics.
Arukuusk, P., Pärnaste, L., Hällbrink, M., & Langel, Ü. (2015). PepFects and NickFects for the Intracellular delivery of nucleic acids. Methods in Molecular Biology, 1324, 303–315.
Arukuusk, P., Pärnaste, L., Oskolkov, N., Copolovici, D. M., Margus, H., Padari, K., et al. (2013). New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. Biochimica et Biophysica Acta, 1828, 1365–1373.
Ashwanikumar, N., Plaut, J. S., Mostofian, B., Patel, S., Kwak, P., Sun, C. (2018). Supramolecular self assembly of nanodrill-like structures for intracellular delivery. Journal of Controlled Release.
Astriab-Fisher, A., Sergueev, D., Fisher, M., Shaw, B. R., & Juliano, R. L. (2002). Conjugates of antisense oligonucleotides with the Tat and antennapedia cell-penetrating peptides: effects on cellular uptake, binding to target sequences, and biologic actions. Pharmaceutical Research, 19, 744–754.
Barnett, E. M., Zhang, X., Maxwell, D., Chang, Q., & Piwnica-Worms, D. (2009). Single-cell imaging of retinal ganglion cell apoptosis with a cell-penetrating, activatable peptide probe in an in vivo glaucoma model. Proceedings of the National Academy of Sciences USA, 106, 9391–9396.
Basu, S., & Wickstrom, E. (1997). Synthesis and characterization of a peptide nucleic acid conjugated to a D-peptide analog of insulin-like growth factor 1 for increased cellular uptake. Bioconjugate Chemistry, 8, 481–488.
Bell, T. J., & Eberwine, J. (2015a). Live cell genomics: Cell-specific transcriptome capture in live tissues and cells. Methods in Molecular Biology, 1324, 447–456.
Bell, T. J., & Eberwine, J. (2015b). Live cell genomics: RNA exon-specific RNA-binding protein isolation. Methods in Molecular Biology, 1324, 457–468.
Bell, T. J., Eiriksdottir, E., Langel, Ü., & Eberwine, J. (2011). PAIR technology: exon-specific RNA-binding protein isolation in live cells. Methods in Molecular Biology, 683, 473–486.
Bell, G. D., Yang, Y., Leung, E., & Krissansen, G. W. (2018). mRNA transfection by a Xentry-protamine cell-penetrating peptide is enhanced by TLR antagonist E6446. PLoS ONE, 13, e0201464.
Bendifallah, N., Rasmussen, F. W., Zachar, V., Ebbesen, P., Nielsen, P. E., & Koppelhus, U. (2006). Evaluation of cell-penetrating peptides (CPPs) as vehicles for intracellular delivery of antisense peptide nucleic acid (PNA). Bioconjugate Chemistry, 17, 750–758.
Benner, N. L., Zang, X., Buehler, D. C., Kickhoefer, V. A., Rome, M. E., Rome, L. H., et al. (2017). Vault nanoparticles: Chemical modifications for imaging and enhanced delivery. ACS Nano, 11, 872–881.
Bennett, C. F., Baker, B. F., Pham, N., Swayze, E., & Geary, R. S. (2016). Pharmacology of antisense drugs. Annual Review of Pharmacology and Toxicology, 10, 10.
Berezikov, E. (2011). Evolution of microRNA diversity and regulation in animals. Nature Reviews Genetics, 12, 846–860.
Bikard, D., Jiang, W., Samai, P., Hochschild, A., Zhang, F., & Marraffini, L. A. (2013). Programmable repression and activation of bacterial gene expression using an engineered CRISPR-Cas system. Nucleic Acids Research, 41, 7429–7437.
Bilan, R., Nabiev, I., & Sukhanova, A. (2016). Quantum dot-based nanotools for bioimaging, diagnostics, and drug delivery. ChemBioChem, 18, 201600357.
Birch, D., Christensen, M. V., Staerk, D., Franzyk, H., & Nielsen, H. M. (2017). Fluorophore labeling of a cell-penetrating peptide induces differential effects on its cellular distribution and affects cell viability. Biochimica et Biophysica Acta, 1859, 2483–2494.
Borgatti, M., Finotti, A., Romanelli, A., Saviano, M., Bianchi, N., Lampronti, I., et al. (2004). Peptide nucleic acids (PNA)-DNA chimeras targeting transcription factors as a tool to modify gene expression. Current Drug Targets, 5, 735–744.
Brandén, L. J., Mohamed, A. J., & Smith, C. I. E. (1999). A peptide nucleic acid-nuclear localization signal fusion that mediates nuclear transport of DNA. Nature Biotechnology, 17, 784–787.
Breger, J. C., Muttenthaler, M., Delehanty, J. B., Thompson, D. A., Oh, E., Susumu, K., et al. (2017). Nanoparticle cellular uptake by dendritic wedge peptides: achieving single peptide facilitated delivery. Nanoscale, 9, 10447–10464.
Brognara, E., Fabbri, E., Aimi, F., Manicardi, A., Bianchi, N., Finotti, A., et al. (2012). Peptide nucleic acids targeting miR-221 modulate p27Kip1 expression in breast cancer MDA-MB-231 cells. International Journal of Oncology, 41, 2119–2127.
Brognara, E., Fabbri, E., Bazzoli, E., Montagner, G., Ghimenton, C., Eccher, A., et al. (2014). Uptake by human glioma cell lines and biological effects of a peptide-nucleic acids targeting miR-221. Journal of Neuro-oncology, 118, 19–28.
Brognara, E., Fabbri, E., Montagner, G., Gasparello, J., Manicardi, A., Corradini, R., et al. (2016). High levels of apoptosis are induced in human glioma cell lines by co-administration of peptide nucleic acids targeting miR-221 and miR-222. International Journal of Oncology, 48, 1029–1038.
Brooks, H., Lebleu, B., & Vives, E. (2005). Tat peptide-mediated cellular delivery: Back to basics. Advanced Drug Delivery Reviews, 57, 559–577.
Byrne, A., Dolan, C., Moriarty, R. D., Martin, A., Neugebauer, U., Forster, R. J., et al. (2015). Osmium(ii) polypyridyl polyarginine conjugate as a probe for live cell imaging; a comparison of uptake, localization and cytotoxicity with its ruthenium(ii) analogue. Dalton Transactions, 44, 14323–14332.
Cardoso, A. M., Trabulo, S., Cardoso, A. L., Lorents, A., Morais, C. M., Gomes, P. (2012). S4(13)-PV cell-penetrating peptide induces physical and morphological changes in membrane-mimetic lipid systems and cell membranes: implications for cell internalization. Biochimica et Biophysica Acta, 1818, 877–88.
Carney, R. P., Thillier, Y., Kiss, Z., Sahabi, A., Heleno Campos, J. C., Knudson, A. ET AL. (2017). Combinatorial library screening with liposomes for discovery of membrane Active Peptides. ACS combinatorial science, 19, 299–307.
Caulier, B., Berthoin, L., Coradin, H., Garban, F., Dagher, M. C., Polack, B., et al. (2017). Targeted release of transcription factors for human cell reprogramming by ZEBRA cell-penetrating peptide. International Journal of Pharmaceutics, 529, 65–74.
Cerrato, C. P., Veiman, K.-L. & Langel, U. (2015). Advances in peptide delivery. Future Science. https://doi.org/10.4155/fseb2013.14.23.
Chang, X., & Hou, Y. (2018). Expression of RecA and cell-penetrating peptide (CPP) fusion protein in bacteria and in mammalian cells. International Journal of Biochemistry and Molecular Biology, 9, 1–10.
Chang, S., Wu, X., Li, Y., Niu, D., Gao, Y., Ma, Z., et al. (2013). A pH-responsive hybrid fluorescent nanoprober for real time cell labeling and endocytosis tracking. Biomaterials, 34, 10182–10190.
Chen, R., Braun, G. B., Luo, X., Sugahara, K. N., Teesalu, T., & Ruoslahti, E. (2013). Application of a proapoptotic peptide to intratumorally spreading cancer therapy. Cancer Research, 73, 1352–1361.
Chen, L., Fang, S., Xiao, X., Zheng, B., & Zhao, M. (2016). Single-stranded DNA assisted cell penetrating peptide-DNA conjugation strategy for intracellular imaging of nucleases. Analytical Chemistry, 88, 11306–11309.
Chen, G., Ma, B., Xie, R., Wang, Y., Dou, K., & Gong, S. (2017). NIR-induced spatiotemporally controlled gene silencing by upconversion nanoparticle-based siRNA nanocarrier. Journal of Controlled Release.
Chen, X., Nomani, A., Patel, N., Nouri, F. S., & Hatefi, A. (2018). Bioengineering a non-genotoxic vector for genetic modification of mesenchymal stem cells. Biomaterials, 152, 1–14.
Chen, B., & Wu, C. (2018). Cationic cell penetrating peptide modified SNARE protein VAMP8 as free chains for gene delivery. Biomaterials Science.
Cheng, C. J., & Saltzman, W. M. (2012). Polymer nanoparticle-mediated delivery of microRNA inhibition and alternative splicing. Molecular Pharmaceutics, 9, 1481–1488.
Cheruku, P., Huang, J. H., Yen, H. J., Iyer, R. S., Rector, K. D., Martinez, J. S., et al. (2015). Tyrosine-derived stimuli responsive, fluorescent amino acids. Chemical Science, 6, 1150–1158.
Cheung, J. C., Kim Chiaw, P., Deber, C. M. & Bear, C. E. (2009). A novel method for monitoring the cytosolic delivery of peptide cargo. Journal of Controlled Release, 137, 2–7.
Choi, S., Jo, J., Seol, D. W., Cha, S. K., Lee, J. E., & Lee, D. R. (2013). Regulation of pluripotency-related genes and differentiation in mouse embryonic stem cells by direct delivery of cell-penetrating peptide-conjugated CARM1 recombinant protein. Balsaenggwa Saengsig, 17, 9–16.
Choi, Y. J., Lee, J. Y., Chung, C. P., & Park, Y. J. (2012). Cell-penetrating superoxide dismutase attenuates oxidative stress-induced senescence by regulating the p53-p21(Cip1) pathway and restores osteoblastic differentiation in human dental pulp stem cells. International Journal of Nanomedicine, 7, 5091–5106.
Chopra, A. (2012). Cy5.5-Conjugated matrix metalloproteinase cleavable peptide nanoprobe. Bethesda (MD): National Center for Biotechnology Information (US).
Chuah, J. A., Yoshizumi, T., Kodama, Y., & Numata, K. (2015). Gene introduction into the mitochondria of Arabidopsis thaliana via peptide-based carriers. Science Report, 5, 7751.
Copolovici, D. M., Langel, K., Eriste, E., & Langel, Ü. (2014). Cell-penetrating peptides: design, synthesis, and applications. ACS Nano, 8, 1972–1994.
Cox, D. B. T., Platt, R. J., & Zhang, F. (2015). Therapeutic genome editing: prospects and challenges. Nature Medicine, 21, 121–131.
Crinelli, R., Bianchi, M., Gentilini, L., Palma, L., & Magnani, M. (2004). Locked nucleic acids (LNA): versatile tools for designing oligonucleotide decoys with high stability and affinity. Current Drug Targets, 5, 745–752.
Crombez, L., Aldrian-Herrada, G., Konate, K., Nguyen, Q. N., McMaster, G. K., Brasseur, R., et al. (2009a). A new potent secondary amphipathic cell-penetrating peptide for siRNA delivery into mammalian cells. Molecular Therapy, 17, 95–103.
Crombez, L., & Divita, G. (2011). A non-covalent peptide-based strategy for siRNA delivery. Methods in Molecular Biology, 683, 349–360.
Crombez, L., Morris, M. C., Dufort, S., Aldrian-Herrada, G., Nguyen, Q., Mc Master, G., et al. (2009b). Targeting cyclin B1 through peptide-based delivery of siRNA prevents tumour growth. Nucleic Acids Research, 37, 4559–4569.
Cui, H., Webber, M. J., & Stupp, S. I. (2010). Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials. Biopolymers, 94, 1–18.
D’Angelo, B., Benedetti, E., Cimini, A., & Giordano, A. (2016). MicroRNAs: a puzzling tool in cancer diagnostics and therapy. Anticancer Research, 36, 5571–5575.
Dasari, B. C., Cashman, S. M., & Kumar-Singh, R. (2017). Reducible PEG-POD/DNA nanoparticles for gene transfer in vitro and in vivo: application in a mouse model of age-related macular degeneration. Molecular Therapy—Nucleic Acids, 8, 77–89.
Dash-Wagh, S., Jacob, S., Lindberg, S., Fridberger, A., Langel, Ü., & Ulfendahl, M. (2012). Intracellular delivery of short interfering RNA in rat organ of corti using a cell-penetrating peptide PepFect6. Molecular Therapy—Nucleic Acids, 1, e61.
D’Astolfo, D. S., Pagliero, R. J., Pras, A., Karthaus, W. R., Clevers, H., Prasad, V., et al. (2015). Efficient intracellular delivery of native proteins. Cell, 161, 674–690.
de Keizer, P. L. (2017). The fountain of youth by targeting senescent cells? Trends in Molecular Medicine, 23, 6–17.
Del’Guidice, T., Lepetit-Stoffaes, J. P., Bordeleau, L. J., Roberge, J., Theberge, V., Lauvaux, C., et al. (2018). Membrane permeabilizing amphiphilic peptide delivers recombinant transcription factor and CRISPR-Cas9/Cpf1 ribonucleoproteins in hard-to-modify cells. PLoS ONE, 13, e0195558.
Demoulins, T., Ebensen, T., Schulze, K., Englezou, P. C., Pelliccia, M., Guzman, C. A., et al. (2017). Self-replicating RNA vaccine functionality modulated by fine-tuning of polyplex delivery vehicle structure. Journal of Controlled Release, 266, 256–271.
di Pisa, M., Chassaing, G., & Swiecicki, J. M. (2015a). Translocation mechanism(s) of cell-penetrating peptides: Biophysical studies using artificial membrane bilayers. Biochemistry, 54, 194–207.
di Pisa, M., Chassaing, G., & Swiecicki, J. M. (2015b). When cationic cell-penetrating peptides meet hydrocarbons to enhance in-cell cargo delivery. Journal of Peptide Science, 21, 356–369.
Diener, C., Garza Ramos Martinez, G., Moreno Blas, D., Castillo Gonzalez, D. A., Corzo, G., Castro-Obregon, S, et al. (2016). Effective design of multifunctional peptides by combining compatible functions. PLoS Computational Biology, 12.
Dobchev, D. A., Mäger, I., Tulp, I., Karelson, G., Tamm, T., Tamm, K., et al. (2010). Prediction of Cell-penetrating peptides using artificial neural networks. Current Computer-Aided Drug Design, 6, 79–89.
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.
Dowaidar, M., Abdelhamid, H. N., Hallbrink, M., Freimann, K., Kurrikoff, K., Zou, X., et al. (2017a). Magnetic nanoparticle assisted self-assembly of cell penetrating peptides-oligonucleotides complexes for gene delivery. Scientific Report, 7, 9159.
Dowaidar, M., Abdelhamid, H. N., Hallbrink, M., Zou, X., & Langel, U. (2017b). Graphene oxide nanosheets in complex with cell penetrating peptides for oligonucleotides delivery. Biochimica et Biophysica Acta, 1861, 2334–2341.
Dowaidar, M., Nasser Abdelhamid, H., Hallbrink, M., Langel, U., & Zou, X. (2018). Chitosan enhances gene delivery of oligonucleotide complexes with magnetic nanoparticles-cell-penetrating peptide. Journal of Biomaterials Applications, 33, 392–401.
Dowdy, S. F. (2017). Overcoming cellular barriers for RNA therapeutics. Nature Biotechnology, 35, 222–229.
Dowdy, S. F., & Levy, M. (2018). RNA therapeutics (almost) comes of age: Targeting, delivery and endosomal escape. Nucleic Acid Therapeutics, 28, 107–108.
Eguchi, A., Meade, B. R., Chang, Y. C., Fredrickson, C. T., Willert, K., Puri, N., et al. (2009). Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nature Biotechnology, 27, 567–571.
Eiriksdottir, E., Mäger, I., Lehto, T., el Andaloussi, S., & Langel, Ü. (2010). Cellular internalization kinetics of (luciferin-)cell-penetrating peptide conjugates. Bioconjugate Chemistry, 21, 1662–1672.
El-Andaloussi, S., Guterstam, P., & Langel, Ü. (2007a). Assessing the delivery efficacy and internalization route of cell-penetrating peptides. Nature Protocols, 2, 2043–2047.
El-Andaloussi, S., Johansson, H. J., Holm, T., & Langel, Ü. (2007b). A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids. Molecular Therapy, 15, 1820–1826.
El-Andaloussi, S., Johansson, H. J., Lundberg, P., & Langel, Ü. (2006). Induction of splice correction by cell-penetrating peptide nucleic acids. The Journal of Gene Medicine, 8, 1262–1273.
El-Andaloussi, S., Johansson, H., Magnusdottir, A., Järver, P., Lundberg, P., & Langel, Ü. (2005). TP10, a delivery vector for decoy oligonucleotides targeting the Myc protein. Journal of Controlled Release, 110, 189–201.
El-Andaloussi, S., Lehto, T., Mäger, I., Rosenthal-Aizman, K., Oprea, I.I., Simonson, O. E., et al. (2011a). Design of a peptide-based vector, PepFect6, for efficient delivery of siRNA in cell culture and systemically in vivo. Nucleic Acids Research, 39, 3972–3987.
El-Andaloussi, S., Said Hassane, F., Boisguerin, P., Sillard, R., Langel, Ü., & Lebleu, B. (2011b). Cell-penetrating peptides-based strategies for the delivery of splice redirecting antisense oligonucleotides. Methods in Molecular Biology, 764, 75–89.
Endoh, T., Sisido, M., & Ohtsuki, T. (2008). Cellular siRNA delivery mediated by a cell-permeant RNA-binding protein and photoinduced RNA interference. Bioconjugate Chemistry, 19, 1017–1024.
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.
Ezzat, K., Andaloussi, S. E., Zaghloul, E. M., Lehto, T., Lindberg, S., Moreno, P. M., et al. (2011). PepFect 14, a novel cell-penetrating peptide for oligonucleotide delivery in solution and as solid formulation. Nucleic Acids Research, 39, 5284–5298.
Fabani, M. M., Abreu-Goodger, C., Williams, D., Lyons, P. A., Torres, A. G., Smith, K. G., et al. (2010). Efficient inhibition of miR-155 function in vivo by peptide nucleic acids. Nucleic Acids Research, 38, 4466–4475.
Fabani, M. M., & Gait, M. J. (2008). miR-122 targeting with LNA/2′-O-methyl oligonucleotide mixmers, peptide nucleic acids (PNA), and PNA-peptide conjugates. RNA, 14, 336–346.
Fabbri, E., Manicardi, A., Tedeschi, T., Sforza, S., Bianchi, N., Brognara, E., et al. (2011). Modulation of the biological activity of microRNA-210 with peptide nucleic acids (PNAs). ChemMedChem, 6, 2192–2202.
Fan, X., Zhang, Y., Liu, X., He, H., Ma, Y., Sun, J., et al. (2016). Biological properties of a 3′,3″-bis-peptide-siRNA conjugate in vitro and in vivo. Bioconjugate Chemistry, 27, 1131–1142.
Fang, W. B., Yao, M., Brummer, G., Acevedo, D., Alhakamy, N., Berkland, C., et al. (2016). Targeted gene silencing of CCL2 inhibits triple negative breast cancer progression by blocking cancer stem cell renewal and M2 macrophage recruitment. Oncotarget, 7.
Favaro, M. T. P., Unzueta, U., de Cabo, M., Villaverde, A., Ferrer-Miralles, N., & Azzoni, A. R. (2018). Intracellular trafficking of a dynein-based nanoparticle designed for gene delivery. European Journal of Pharmaceutical Sciences, 112, 71–78.
Favretto, M. E., & Brock, R. (2015). Stereoselective uptake of cell-penetrating peptides is conserved in antisense oligonucleotide polyplexes. Small (Weinheim an der Bergstrasse, Germany), 11, 1414–1417.
Fellmann, C., Gowen, B. G., Lin, P. C., Doudna, J. A., & Corn, J. E. (2016). Cornerstones of CRISPR-Cas in drug discovery and therapy. Nature Reviews Drug Discovery, 23, 238.
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, R. K., Mattern-Schain, S. I., Best, M. D., Kirkpatrick, S. S., Freeman, M. B., Grandas, O. H., et al. (2017). Improving the efficacy of liposome-mediated vascular gene therapy via lipid surface modifications. Journal of Surgical Research, 219, 136–144.
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.
Fossat, P., Dobremez, E., Bouali-Benazzouz, R., Favereaux, A., Bertrand, S. S., Kilk, K., et al. (2010). Knockdown of L calcium channel subtypes: differential effects in neuropathic pain. Journal of Neuroscience, 30, 1073–1085.
Fraser, G. L., Holmgren, J., Clarke, P. B., & Wahlestedt, C. (2000). Antisense inhibition of delta-opioid receptor gene function in vivo by peptide nucleic acids. Molecular Pharmacology, 57, 725–731.
Freimann, K., Arukuusk, P., Kurrikoff, K., Parnaste, L., Raid, R., Piirsoo, A., et al. (2018). Formulation of stable and homogeneous cell-penetrating peptide NF55 nanoparticles for efficient gene delivery in vivo. Molecular Therapy—Nucleic Acids, 10, 28–35.
Freimann, K., Arukuusk, K., Kurrikoff, K., Vasconselos, L. D. F., Veiman, K.-L., Uusna, J. (2016). Optimization of in vivo pDNA gene delivery with NickFect peptide vectors. Journal of Controlled Release, 241, 135–143.
Freire, J. M., Rego De Figueiredo, I., Valle, J., Veiga, A. S., Andreu, D., Enguita, et al. (2017). siRNA-cell-penetrating peptides complexes as a combinatorial therapy against chronic myeloid leukemia using BV173 cell line as model. Journal of Controlled Release, 245, 127–136.
Freire, J. M., Veiga, A. S., Rego De Figueiredo, I., De La Torre, B. G., Santos, N. C., Andreu, D., et al. (2014). Nucleic acid delivery by cell penetrating peptides derived from dengue virus capsid protein: Design and mechanism of action. FEBS Journal, 281, 191–215.
Friedman, A. A., Letai, A., Fisher, D. E., & Flaherty, K. T. (2015). Precision medicine for cancer with next-generation functional diagnostics. Nature Reviews Cancer, 15, 747–756.
Futaki, S., Ohashi, W., Suzuki, T., Niwa, M., Tanaka, S., Ueda, K., et al. (2001). Stearylated arginine-rich peptides: A new class of transfection systems. Bioconjugate Chemistry, 12, 1005–1011.
Gagat, M., Zielinska, W., & Grzanka, A. (2017). Cell-penetrating peptides and their utility in genome function modifications (Review). International Journal of Molecular Medicine, 40, 1615–1623.
Gaj, T., Sirk, S. J., Shui, S. L., & Liu, J. (2016). Genome-editing technologies: Principles and applications. Cold Spring Harbor Perspectives in Biology, 8.
Ganguly, S., Chaubey, B., Tripathi, S., Upadhyay, A., Neti, P. V., Howell, R. W., et al. (2008). Pharmacokinetic analysis of polyamide nucleic-acid-cell penetrating peptide conjugates targeted against HIV-1 transactivation response element. Oligonucleotides, 18, 277–286.
Ganju, A., Khan, S., Hafeez, B. B., Behrman, S. W., Yallapu, M. M., Chauhan, S. C., et al. (2016). miRNA nanotherapeutics for cancer. Drug Discov Today, 1, 30408-1.
Gautam, A., Sharma, M., Vir, P., Chaudhary, K., Kapoor, P., Kumar, R., et al. (2015). Identification and characterization of novel protein-derived arginine-rich cell-penetrating peptides. European Journal of Pharmaceutics and Biopharmaceutics, 89, 93–106.
Gautam, A., Singh, H., Tyagi, A., Chaudhary, K., Kumar, R., Kapoor, P., et al. (2012). CPPsite: A curated database of cell penetrating peptides. Database (Oxford), bas015.
Geiler, C., Andrade, I., & Greenwald, D. (2014). Exogenous c-Myc Blocks differentiation and improves expansion of human erythroblasts in vitro. International Journal of Stem Cells, 7, 153–157.
Golan, M., Feinshtein, V., & David, A. (2016). Conjugates of HA2 with octaarginine-grafted HPMA copolymer offer effective siRNA delivery and gene silencing in cancer cells. European Journal of Pharmaceutics and Biopharmaceutics, 109, 103–112.
Good, L., Awasthi, S. K., Dryselius, R., Larsson, O., & Nielsen, P. E. (2001). Bactericidal antisense effects of peptide-PNA conjugates. Nature Biotechnology, 19, 360–364.
Gratton, J. P., Yu, J., Griffith, J. W., Babbitt, R. W., Scotland, R. S., Hickey, R., et al. (2003). Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-deficient viruses in cells and in vivo. Nature Medicine, 9, 357–362.
Guo, Z., Peng, H., Kang, J., & Sun, D. (2016). Cell-penetrating peptides: Possible transduction mechanisms and therapeutic applications. Biomedical Reports, 4, 528–534.
Guo, J., Wang, H., & Hu, X. (2013). Reprogramming and transdifferentiation shift the landscape of regenerative medicine. DNA and Cell Biology, 32, 565–572.
Gupta, A., Mishra, A., & Puri, N. (2017). Peptide nucleic acids: Advanced tools for biomedical applications. Journal of Biotechnology, 259, 148–159.
Gupta, S. K., & Shukla, P. (2016). Gene editing for cell engineering: trends and applications. Critical Reviews in Biotechnology, 18, 1–13.
Ha, J. S., Byun, J., & Ahn, D. R. (2016). Overcoming doxorubicin resistance of cancer cells by Cas9-mediated gene disruption. Scientific Report, 6, 22847.
Hällbrink, M., Floren, A., Elmquist, A., Pooga, M., Bartfai, T., & Langel, Ü. (2001). Cargo delivery kinetics of cell-penetrating peptides. Biochimica et Biophysica Acta, 1515, 101–109.
Hällbrink, M., & Karelson, M. (2015). Prediction of cell-penetrating peptides. Methods in Molecular Biology, 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., & Langel, Ü. (2006). Prediction of cell-penetrating peptides and prodrug approach. In Ü. Langel (Ed.), Handbook of cell-penetrating peptides (2nd ed., pp. 77–85). Boca Raton, London, New York: CRC Press/Taylor & Francis.
Hällbrink, M., Saar, K., Östenson, C. G., Soomets, U., Efendic, S., Howl, J., et al. (1999). Effects of vasopressin-mastoparan chimeric peptides on insulin release and G-protein activity. Regulatory Peptides, 82, 45–51.
Hammond, S. M., Hazell, G., Shabanpoor, F., Saleh, A. F., Bowerman, M., Sleigh, J. N., et al. (2016). Systemic peptide-mediated oligonucleotide therapy improves long-term survival in spinal muscular atrophy. Proceedings of the National Academy of Sciences USA, 113, 10962–10967.
Hansen, M., Kilk, K., & Langel, Ü. (2008). Predicting cell-penetrating peptides. Advanced Drug Delivery Reviews, 60, 572–579.
Harreither, E., Rydberg, H. A., Amand, H. L., Jadhav, V., Fliedl, L., Benda, C., et al. (2014). Characterization of a novel cell penetrating peptide derived from human Oct4. Cell Regen (Lond), 3, 2.
Hattori, T., Okitsu, K., Yamazaki, N., Ohoka, N., Shibata, N., Misawa, T., et al. (2017). Simple and efficient knockdown of His-tagged proteins by ternary molecules consisting of a His-tag ligand, a ubiquitin ligase ligand, and a cell-penetrating peptide. Bioorganic & Medicinal Chemistry Letters, 27, 4478–4481.
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.
He, Y., Li, F., & Huang, Y. (2018). Smart cell-penetrating peptide-based techniques for intracellular delivery of therapeutic macromolecules. Advances in Protein Chemistry and Structural Biology, 112, 183–220.
Helmfors, H., Eriksson, J., & Langel, Ü. (2015). Optimized luciferase assay for cell-penetrating peptide-mediated delivery of short oligonucleotides. Analytical Biochemistry, 484, 136–142.
Heng, B. C., & Fussenegger, M. (2014). Integration-free reprogramming of human somatic cells to induced pluripotent stem cells (iPSCs) without viral vectors, recombinant DNA, and genetic modification. Methods in Molecular Biology, 0554-6_6.
Herbig, M. E., Fromm, U., Leuenberger, J., Krauss, U., Beck-Sickinger, A. G., & Merkle, H. P. (2005). Bilayer interaction and localization of cell penetrating peptides with model membranes: a comparative study of a human calcitonin (hCT)-derived peptide with pVEC and pAntp(43-58). Biochimica et Biophysica Acta, 1712, 197–211.
Hirai, T., Yamagishi, Y., Koizumi, N., Nonaka, M., Mochida, R., Shida, K., et al. (2017). Identification of adenovirus-derived cell-penetrating peptide. Biological & Pharmaceutical Bulletin, 40, 195–204.
Howl, J., & Jones, S. (2015a). Cell penetrating peptide-mediated transport enables the regulated secretion of accumulated cargoes from mast cells. Journal of Controlled Release, 202, 108–117.
Howl, J., & Jones, S. (2015b). Insights into the molecular mechanisms of action of bioportides: A strategy to target protein-protein interactions. Expert Reviews in Molecular Medicine, 17, e1.
Howl, J., & Jones, S. (2015c). Protein mimicry and the design of bioactive cell-penetrating peptides. Methods in Molecular Biology, 1324, 177–190.
Howl, J., Langel, Ü., Hawtin, S. R., Valkna, A., Yarwood, N. J., Saar, K., et al. (1997). Chimeric strategies for the rational design of bioactive analogs of small peptide hormones. FASEB Journal, 11, 582–590.
Hsu, P. D., Scott, D. A., Weinstein, J. A., Ran, F. A., Konermann, S., Agarwala, V., et al. (2013). DNA targeting specificity of RNA-guided Cas9 nucleases. Nature Biotechnology, 31, 827–832.
Hu, Q., Chen, R., Teesalu, T., Ruoslahti, E., & Clegg, D. O. (2014). Reprogramming human retinal pigmented epithelial cells to neurons using recombinant proteins. Stem Cells Translational Medicine, 3, 1526–1534.
Hu, Q. L., Jiang, Q. Y., Jin, X., Shen, J., Wang, K., Li, Y. B., et al. (2013). Cationic microRNA-delivering nanovectors with bifunctional peptides for efficient treatment of PANC-1 xenograft model. Biomaterials, 34, 2265–2276.
Hyrup Moller, L., Bahnsen, J. S., Nielsen, H. M., Ostergaard, J., Sturup, S., & Gammelgaard, B. (2015). Selenium as an alternative peptide label - comparison to fluorophore-labelled penetratin. European Journal of Pharmaceutical Sciences, 67, 76–84.
Hyun, S., Choi, Y., Lee, H. N., Lee, C., Oh, D., Lee, D. K., et al. (2018). Construction of histidine-containing hydrocarbon stapled cell penetrating peptides for in vitro and in vivo delivery of siRNAs. Chemical Science, 9, 3820–3827.
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.
Hyvonen, M., & Laakkonen, P. (2015). Identification and characterization of homing peptides using in vivo peptide phage display. Methods in Molecular Biology, 1324, 205–222.
Ifediba, M. A., Medarova, Z., Ng, S. W., Yang, J., & Moore, A. (2010). siRNA delivery to CNS cells using a membrane translocation peptide. Bioconjugate Chemistry, 21, 803–806.
Ignatovich, I. A., Dizhe, E. B., Pavlotskaya, A. V., Akifiev, B. N., Burov, S. V., Orlov, S. V., et al. (2003). Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat Protein are transferred to mammalian cells by endocytosis-mediated pathways. Journal of Biological Chemistry, 278, 42625–42636.
Illien, F., Rodriguez, N., Amoura, M., Joliot, A., Pallerla, M., Cribier, S., et al. (2016). Quantitative fluorescence spectroscopy and flow cytometry analyses of cell-penetrating peptides internalization pathways: optimization, pitfalls, comparison with mass spectrometry quantification. Scienfic Report, 6.
Imani, R., Emami, S. H., & Faghihi, S. (2015). Synthesis and characterization of an octaarginine functionalized graphene oxide nano-carrier for gene delivery applications. Physical Chemistry Chemical Physics: PCCP, 17, 6328–6339.
Imani, R., Prakash, S., Vali, H., & Faghihi, S. (2018). Polyethylene glycol and octa-arginine dual-functionalized nanographene oxide: An optimization for efficient nucleic acid delivery. Biomaterials Science, 6, 1636–1650.
Imani, R., Shao, W., Taherkhani, S., Emami, S. H., Prakash, S., & Faghihi, S. (2016). Dual-functionalized graphene oxide for enhanced siRNA delivery to breast cancer cells. Colloids and Surfaces B: Biointerfaces, 147, 315–325.
Ishiguro, S., Alhakamy, N. A., Uppalapati, D., Delzeit, J., Berkland, C. J., & Tamura, M. (2016). 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, 18, 41686-2.
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.
Jearawiriyapaisarn, N., Moulton, H. M., Buckley, B., Roberts, J., Sazani, P., Fucharoen, S., et al. (2008). Sustained dystrophin expression induced by peptide-conjugated morpholino oligomers in the muscles of mdx mice. Molecular Therapy, 16, 1624–1629.
Jeong, C., Yoo, J., Lee, D., & Kim, Y. C. (2016). A branched TAT cell-penetrating peptide as a novel delivery carrier for the efficient gene transfection. Biomaterials Research, 20, 28.
Ji, X., Lv, H., Guo, J., Ding, C., & Luo, X. (2018). A DNA nanotube-peptide biocomplex for mRNA detection and its application in cancer diagnosis and targeted therapy. Chemistry.
Jones, L. R., Goun, E. A., Shinde, R., Rothbard, J. B., Contag, C. H., & Wender, P. A. (2006). Releasable luciferin-transporter conjugates: tools for the real-time analysis of cellular uptake and release. Journal of the American Chemical Society, 128, 6526–6527.
Jung, H., Kim, D. O., Byun, J. E., Kim, W. S., Kim, M. J., Song, H. Y., et al. (2016). Thioredoxin-interacting protein regulates haematopoietic stem cell ageing and rejuvenation by inhibiting p 38 kinase activity. Nature Communications, 7.
Jung, M. R., Shim, I. K., Kim, E. S., Park, Y. J., Yang, Y. I., Lee, S. K., et al. (2011). Controlled release of cell-permeable gene complex from poly(L-lactide) scaffold for enhanced stem cell tissue engineering. Journal of Controlled Release, 152, 294–302.
Kadkhodayan, S., Jafarzade, B. S., Sadat, S. M., Motevalli, F., Agi, E., & Bolhassani, A. (2017). Combination of cell penetrating peptides and heterologous DNA prime/protein boost strategy enhances immune responses against HIV-1 Nef antigen in BALB/c mouse model. Immunology Letters, 188, 38–45.
Kadkhodayan, S., Sadat, S. M., Irani, S., Fotouhi, F., & Bolhassani, A. (2016). Generation of GFP native protein for detection of its intracellular uptake by cell-penetrating peptides. Folia Biologica, 62, 103–109.
Kaitsuka, T., Noguchi, H., Shiraki, N., Kubo, T., Wei, F. Y., Hakim, F., et al. (2014). Generation of functional insulin-producing cells from mouse embryonic stem cells through 804G cell-derived extracellular matrix and protein transduction of transcription factors. Stem Cells Transl Med, 3, 114–127.
Kaitsuka, T., & Tomizawa, K. (2015). Cell-penetrating peptide as a means of directing the differentiation of induced-pluripotent stem cells. International Journal of Molecular Sciences, 16, 26667–26676.
Kalafatovic, D., & Giralt, E. (2017). Cell-penetrating peptides: Design strategies beyond primary structure and amphipathicity. Molecules, 22.
Kam, Y., Rubinstein, A., Naik, S., Djavsarov, I., Halle, D., Ariel, I., et al. (2014). Detection of a long non-coding RNA (CCAT1) in living cells and human adenocarcinoma of colon tissues using FIT-PNA molecular beacons. Cancer Letters, 352, 90–96.
Kamei, N., Shingaki, T., Kanayama, Y., Tanaka, M., Zochi, R., Hasegawa, K., et al. (2016). Visualization and quantitative assessment of the brain distribution of insulin through nose-to-brain delivery based on the cell-penetrating peptide noncovalent strategy. Molecular Pharmaceutics, 13, 1004–1011.
Kameyama, S., Horie, M., Kikuchi, T., Omura, T., Takeuchi, T., Nakase, I., et al. (2006). Effects of cell-permeating peptide binding on the distribution of 125I-labeled Fab fragment in rats. Bioconjugate Chemistry, 17, 597–602.
Kang, S. H., Cho, M. J., & Kole, R. (1998). Up-regulation of luciferase gene expression with antisense oligonucleotides: Implications and applications in functional assay development. Biochemistry, 37, 6235–6239.
Karagiannis, E. D., Alabi, C. A., & Anderson, D. G. (2012). Rationally designed tumor-penetrating nanocomplexes. ACS Nano, 6, 8484–8487.
Karas, J., Turner, B. J., & Shabanpoor, F. (2018). The assembly of fluorescently labeled peptide-oligonucleotide conjugates via orthogonal ligation strategies. Methods in Molecular Biology, 1828, 355–363.
Kato, T., Yamashita, H., Misawa, T., Nishida, K., Kurihara, M., Tanaka, M., et al. (2016). Plasmid DNA delivery by arginine-rich cell-penetrating peptides containing unnatural amino acids. Bioorganic & Medicinal Chemistry, 24, 2681–2687.
Kauffman, W. B., Guha, S., & Wimley, W. C. (2018). Synthetic molecular evolution of hybrid cell penetrating peptides. Nature Communications, 9, 2568.
Keller, A. A., Breitling, R., Hemmerich, P., Kappe, K., Braun, M., Wittig, B., et al. (2014). Transduction of proteins into leishmania tarentolae by formation of non-covalent complexes with cell-penetrating peptides. Journal of Cellular Biochemistry, 115, 243–252.
Khalil, I. A., & Harashima, H. (2018). An efficient pegylated gene delivery system with improved targeting: Synergism between octaarginine and a fusogenic peptide. International Journal of Pharmaceutics.
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.
Khalil, I. A., Kimura, S., Sato, Y., & Harashima, H. (2018). Synergism between a cell penetrating peptide and a pH-sensitive cationic lipid in efficient gene delivery based on double-coated nanoparticles. Journal of Controlled Release, 275, 107–116.
Kilk, K., el Andaloussi, S., Järver, P., Meikas, A., Valkna, A., Bartfai, T., et al. (2005). Evaluation of transportan 10 in PEI mediated plasmid delivery assay. Journal of Controlled Release, 103, 511–523.
Kim, D. H., & Choi, J. M. (2018). Chitinase 3-like-1, a novel regulator of Th1/CTL responses, as a therapeutic target for increasing anti-tumor immunity. BMB Reports.
Kim, D., Lee, Y., Dreher, T. W., & Cho, T. J. (2018). Empty Turnip yellow mosaic virus capsids as delivery vehicles to mammalian cells. Virus Research.
Kiss, E., Gyulai, G., Pari, E., Horvati, K., & Bosze, S. (2018). Membrane affinity and fluorescent labelling: comparative study of monolayer interaction, cellular uptake and cytotoxicity profile of carboxyfluorescein-conjugated cationic peptides. Amino Acids.
Knight, J. C., Topping, C., Mosley, M., Kersemans, V., Falzone, N., Fernandez-Varea, J. M., et al. (2015). PET imaging of DNA damage using (89)Zr-labelled anti-gammaH2AX-TAT immunoconjugates. European Journal of Nuclear Medicine and Molecular Imaging, 42, 1707–1717.
Kobayashi, H., Misawa, T., Oba, M., Hirata, N., Kanda, Y., Tanaka, M., et al. (2018). Structural development of cell-penetrating peptides containing cationic proline derivatives. Chemical and Pharmaceutical Bulletin (Tokyo), 66, 575–580.
Komor, A. C., Badran, A. H., & Liu, D. R. (2016). CRISPR-based technologies for the manipulation of eukaryotic genomes. Cell, 15, 31465–31469.
Konate, K., Rydstrom, A., Divita, G., & Deshayes, S. (2013). Everything you always wanted to know about CADY-mediated siRNA delivery* (* but afraid to ask). Current Pharmaceutical Design, 19, 2869–2877.
Kostiv, U., Kotelnikov, I., Proks, V., Slouf, M., Kucka, J., Engstova, H., et al. (2016). RGDS- and TAT-conjugated upconversion of NaYF4:Yb(3+)/Er(3+)&SiO2 nanoparticles. In vitro human epithelioid cervix carcinoma cellular uptake, imaging, and targeting. ACS Applied Materials & Interfaces, 8, 20422–20431.
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.
Kumar, V., Agrawal, P., Kumar, R., Bhalla, S., Usmani, S. S., Varshney, G. C., et al. (2018). Prediction of cell-penetrating potential of modified peptides containing natural and chemically modified residues. Frontiers in Microbiology, 9, 725.
Kurrikoff, K., Gestin, M., & Langel, Ü. (2016). Recent in vivo advances in cell-penetrating peptide-assisted drug delivery. Expert Opinion on Drug Delivery, 13, 373–387.
Kurrikoff, K., Veiman, K. L., Kunnapuu, K., Peets, E. M., Lehto, T., Parnaste, L., et al. (2017). Effective in vivo gene delivery with reduced toxicity, achieved by charge and fatty acid -modified cell penetrating peptide. Scientific Report, 7, 17056.
Kurrikoff, K., Veiman, K.-L., & Langel, Ü. (2015). CPP-based delivery system for in vivo gene delivery. Methods in Molecular Biology, 1324, 339–347.
Kyrychenko, A., Rodnin, M. V., & Ladokhin, A. S. (2015). Calibration of distribution analysis of the depth of membrane penetration using simulations and depth-dependent fluorescence quenching. Journal of Membrane Biology, 248, 583–594.
Ladokhin, A. S. (2014). Measuring membrane penetration with depth-dependent fluorescence quenching: distribution analysis is coming of age. Biochimica et Biophysica Acta, 9, 1.
Langel, Ü., Land, T., & Bartfai, T. (1992). Design of chimeric peptide ligands to galanin receptors and substance P receptors. International Journal of Peptide and Protein Research, 39, 516–522.
Langel, Ü., Pooga, M., Kairane, C., Zilmer, M., & Bartfai, T. (1996). A galanin-mastoparan chimeric peptide activates the Na+, K(+)-ATPase and reverses its inhibition by ouabain. Regulatory Peptides, 62, 47–52.
Lee, J., & Bogyo, M. (2010). Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumain. ACS Chemical Biology, 5, 233–243.
Lee, E. Y., Fulan, B. M., Wong, G. C., & Ferguson, A. L. (2016). Mapping membrane activity in undiscovered peptide sequence space using machine learning. Proceedings of the National Academy of Sciences USA, 14, 201609893.
Lee, J., Moon, S. U., Lee, Y. S., Ali, B. A., Al-Khedhairy, A. A., Ali, D., et al. (2015) Quantum dot-based molecular beacon to monitor intracellular microRNAs. Sensors (Basel), 15, 12872–12883.
Lee, J., Sayed, N., Hunter, A., Au, K. F., Wong, W. H., Mocarski, E. S., et al. (2012). Activation of innate immunity is required for efficient nuclear reprogramming. Cell, 151, 547–558.
Lehto, T., Abes, R., Oskolkov, N., Suhorutsenko, J., Copolovici, D. M., Mäger, I., et al. (2010). Delivery of nucleic acids with a stearylated (RxR)4 peptide using a non-covalent co-incubation strategy. Journal of Controlled Release, 141, 42–51.
Lehto, T., Ezzat, K., Wood, M. J., & el Andaloussi, S. (2016). Peptides for nucleic acid delivery. Advanced Drug Delivery Reviews, 106, 172–182.
Lehto, T., Vasconcelos, L., Margus, H., Figueroa, R., Pooga, M., Hällbrink, M., et al. (2017). Saturated fatty acid analogues of cell-penetrating peptide PepFect14: Role of fatty acid modification in complexation and delivery of splice-correcting oligonucleotides. Bioconjugate Chemistry, 28, 782–792.
Lei, Y., Tang, H., Yao, L., Yu, R., Feng, M., & Zou, B. (2008). Applications of mesenchymal stem cells labeled with Tat peptide conjugated quantum dots to cell tracking in mouse body. Bioconjugate Chemistry, 19, 421–427.
Levacic, A. K., Morys, S., Kempter, S., Lachelt, U., & Wagner, E. (2017). Minicircle versus plasmid DNA delivery by receptor-targeted polyplexes. Human Gene therapy, 28, 862–874.
Li, S., Kim, S. Y., Pittman, A. E., King, G. M., Wimley, W. C., & Hristova, K. (2018). Potent macromolecule-sized poration of lipid bilayers by the macrolittins, A synthetically evolved family of pore-forming peptides. Journal of the American Chemicals.
Li, H., & Tsui, T. (2015). Six-cell penetrating peptide-based fusion proteins for siRNA delivery. Drug Delivery, 22, 436–443.
Li, H., Zheng, X., Koren, V., Vashist, Y. K., & Tsui, T. Y. (2014). Highly efficient delivery of siRNA to a heart transplant model by a novel cell penetrating peptide-dsRNA binding domain. International Journal of Pharmaceutics, 469, 206–213.
Lim, J., Kim, J., Kang, J., & JO, D. (2014). Partial somatic to stem cell transformations induced by cell-permeable reprogramming factors. Scientific Report, 4.
Lindberg, S., Munoz-Alarcon, A., Helmfors, H., Mosqueira, D., Gyllborg, D., Tudoran, O., et al. (2013). PepFect15, a novel endosomolytic cell-penetrating peptide for oligonucleotide delivery via scavenger receptors. International Journal of Pharmaceutics, 441, 242–247.
Lindgren, M., Gallet, X., Soomets, U., Hällbrink, M., Brakenhielm, E., Pooga, M., et al. (2000). Translocation properties of novel cell penetrating transportan and penetratin analogues. Bioconjugate Chemistry, 11, 619–626.
Liu, X., Braun, G. B., Qin, M., Ruoslahti, E., & Sugahara, K. N. (2017). In vivo cation exchange in quantum dots for tumor-specific imaging. Nature Communications, 8, 343.
Liu, J., Gaj, T., Yang, Y., Wang, N., Shui, S., Kim, S., et al. (2015). Efficient delivery of nuclease proteins for genome editing in human stem cells and primary cells. Nature Protocols, 10, 1842–1859.
Liu, M., Guo, Y. M., Wu, Q. F., Yang, J. L., Wang, P., Wang, S. C., et al. (2006). Paramagnetic particles carried by cell-penetrating peptide tracking of bone marrow mesenchymal stem cells, a research in vitro. Biochemical and Biophysical Research Communications, 347, 133–140.
Liu, B. R., Huang, Y. W., Chiang, H. J., & Lee, H. J. (2010). Cell-penetrating peptide-functionalized quantum dots for intracellular delivery. Journal of Nanoscience and Nanotechnology, 10, 7897–7905.
Liu, Y., Wu, X., Gao, Y., Zhang, J., Zhang, D., Gu, S., et al. (2016a). Aptamer-functionalized peptide H3CR219C as a novel nanovehicle for codelivery of fasudil and miRNA-195 targeting hepatocellular carcinoma. International Journal of Nanomedicine, 11, 3891–3905.
Liu, H., Zeng, F., Zhang, M., Huang, F., Wang, J., Guo, J., et al. (2016b). Emerging landscape of cell penetrating peptide in reprogramming and gene editing. Journal of Controlled Release, 226, 124–137.
Lönn, P., & Dowdy, S. F. (2015). Cationic PTD/CPP-mediated macromolecular delivery: Charging into the cell. Expert opinion on drug delivery, 12, 1627–1636.
Lorenzetto, E., Ettorre, M., Pontelli, V., Bolomini-Vittori, M., Bolognin, S., Zorzan, S., et al. (2013). Rac1 selective activation improves retina ganglion cell survival and regeneration. PLoS One, 8.
Lostale-Seijo, I., Louzao, I., Juanes, M., & Montenegro, J. (2017). Peptide/Cas9 nanostructures for ribonucleoprotein cell membrane transport and gene edition. Chemical Science, 8, 7923–7931.
Lou, G., Zhang, Q., Xiao, F., Xiang, Q., Su, Z., Zhang, L., et al. (2012). Intranasal administration of TAT-haFGF((1)(4)(-)(1)(5)(4)) attenuates disease progression in a mouse model of Alzheimer’s disease. Neuroscience, 223, 225–237.
Lovatt, D., Ruble, B. K., Lee, J., Dueck, H., Kim, T. K., Fisher, S., et al. (2014). Transcriptome in vivo analysis (TIVA) of spatially defined single cells in live tissue. Nature Methods, 11, 190–196.
Lundberg, P., el Andaloussi, S., Sutlu, T., Johansson, H., & Langel, Ü. (2007). Delivery of short interfering RNA using endosomolytic cell-penetrating peptides. FASEB Journal, 21, 2664–2671.
Ma, W., Jin, G. W., Gehret, P. M., Chada, N. C., & Suh, W. H. (2018). A novel cell penetrating peptide for the differentiation of human neural stem cells. Biomolecules, 8.
Mäe, M., el Andaloussi, S., Lundin, P., Oskolkov, N., Johansson, H. J., Guterstam, P., et al. (2009). A stearylated CPP for delivery of splice correcting oligonucleotides using a non-covalent co-incubation strategy. Journal of Controlled Release, 134, 221–227.
Mäger, I., Eiriksdottir, E., Langel, K., el Andaloussi, S., & Langel, Ü. (2010). Assessing the uptake kinetics and internalization mechanisms of cell-penetrating peptides using a quenched fluorescence assay. Biochimica et Biophysica Acta, 1798, 338–343.
Mäger, I., Langel, K., Lehto, T., Eiriksdottir, E., & Langel, Ü. (2012). The role of endocytosis on the uptake kinetics of luciferin-conjugated cell-penetrating peptides. Biochimica et Biophysica Acta, 1818, 502–511.
Magzoub, M., Eriksson, L. E., & Graslund, A. (2003). Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles. Biophysical Chemistry, 103, 271–288.
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.
Manavalan, B., Subramaniyam, S., Shin, T. H., Kim, M., O. & Lee, G. (2018). Machine-learning-based prediction of cell-penetrating peptides and their uptake efficiency with improved accuracy. Journal of Proteome Research.
Manceur, A., Wu, A., & Audet, J. (2007). Flow cytometric screening of cell-penetrating peptides for their uptake into embryonic and adult stem cells. Analytical Biochemistry, 364, 51–59.
Manicardi, A., Fabbri, E., Tedeschi, T., Sforza, S., Bianchi, N., Brognara, E., et al. (2012). Cellular uptakes, biostabilities and anti-miR-210 activities of chiral arginine-PNAs in leukaemic K562 cells. ChemBioChem, 13, 1327–1337.
Mann, A., Thakur, G., Shukla, V., Singh, A. K., Khanduri, R., Naik, R., et al. (2011). Differences in DNA condensation and release by lysine and arginine homopeptides govern their DNA delivery efficiencies. Molecular Pharmaceutics, 8, 1729–1741.
Margus, H., Arukuusk, P., Langel, U., & Pooga, M. (2016). Characteristics of cell-penetrating peptide/nucleic acid nanoparticles. Molecular Pharmaceutics, 13, 172–179.
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.
Martins, I. M., Reis, R. L., & Azevedo, H. S. (2016). Phage display technology in biomaterials engineering: Progress and opportunities for applications in regenerative medicine. ACS Chemical Biology, 10, 10.
Mathupala, S. P. (2009). Delivery of small-interfering RNA (siRNA) to the brain. Expert Opinion on Therapeutic Patents, 19, 137–140.
Maxwell, D., Chang, Q., Zhang, X., Barnett, E. M., & Piwnica-Worms, D. (2009). An improved cell-penetrating, caspase-activatable, near-infrared fluorescent peptide for apoptosis imaging. Bioconjugate Chemistry, 20, 702–709.
McCarthy, H. O., McCaffrey, J., McCrudden, C. M., Zholobenko, A., Ali, A. A., McBride, J. W., et al. (2014). Development and characterization of self-assembling nanoparticles using a bio-inspired amphipathic peptide for gene delivery. Journal of Controlled Release, 189, 141–149.
McClorey, G., & Banerjee, S. (2018). Cell-penetrating peptides to enhance delivery of oligonucleotide-based therapeutics. Biomedicines, 6.
Meade, B. R., & Dowdy, S. F. (2007). Exogenous siRNA delivery using peptide transduction domains/cell penetrating peptides. Advanced Drug Delivery Reviews, 59, 134–140.
Medema, R. H., Kops, G. J. P. L., Bos, J. L., & Burgering, B. M. T. (2000). AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27(kip1). Nature, 404, 782–787.
Medintz, I. L., Pons, T., Delehanty, J. B., Susumu, K., Brunel, F. M., Dawson, P. E., et al. (2008). Intracellular delivery of quantum dot-protein cargos mediated by cell penetrating peptides. Bioconjugate Chemistry, 19, 1785–1795.
Medintz, I. L., Uyeda, H. T., Goldman, E. R., & Mattoussi, H. (2005). Quantum dot bioconjugates for imaging, labelling and sensing. Nature Materials, 4, 435–446.
Meerovich, I., Muthukrishnan, N., Johnson, G. A., Erazo-Oliveras, A., & Pellois, J. P. (2014). Photodamage of lipid bilayers by irradiation of a fluorescently labeled cell-penetrating peptide. Biochimica et Biophysica Acta, 1840, 507–515.
Meng, Z., Guo, L., & Li, Q. (2017). Peptide-coated semiconductor polymer dots for stem cells labeling and tracking. Chemistry, 23, 6836–6844.
Meng, Z., Kang, Z., Sun, C., Yang, S., Zhao, B., Feng, S., et al. (2018). Enhanced gene transfection efficiency by use of peptide vectors containing laminin receptor-targeting sequence YIGSR. Nanoscale, 10, 1215–1227.
Mesken, J., Iltzsche, A., Mulac, D., & Langer, K. (2017). Modifying plasmid-loaded HSA-nanoparticles with cell penetrating peptides—Cellular uptake and enhanced gene delivery. International Journal of Pharmaceutics, 522, 198–209.
Michiue, H., Eguchi, A., Scadeng, M., & Dowdy, S. F. (2009). Induction of in vivo synthetic lethal RNAi responses to treat glioblastoma. Cancer Biology & Therapy, 8, 2306–2313.
Mitra, R. N., Zheng, M., Weiss, E. R., & Han, Z. (2018). Genomic form of rhodopsin DNA nanoparticles rescued autosomal dominant Retinitis pigmentosa in the P23H knock-in mouse model. Biomaterials, 157, 26–39.
Mitsueda, A., Shimatani, Y., Ito, M., Ohgita, T., Yamada, A., Hama, S., et al. (2013). Development of a novel nanoparticle by dual modification with the pluripotential cell-penetrating peptide PepFect6 for cellular uptake, endosomal escape, and decondensation of an siRNA core complex. Biopolymers, 100, 698–704.
Mondhe, M., Chessher, A., Goh, S., Good, L., & Stach, J. E. (2014). Species-selective killing of bacteria by antimicrobial peptide-PNAs. PLoS ONE, 9, e89082.
Morales, D. P., Wonderly, W. R., Huang, X., McAdams, M., Chron, A. B., & Reich, N. O. (2017). Affinity-based assembly of peptides on plasmonic nanoparticles delivered intracellularly with light activated control. Bioconjugate Chemistry, 28, 1816–1820.
Morris, M. C., Chaloin, L., Méry, J., Heitz, F., & Divita, G. (1999). A novel potent strategy for gene delivery using a single peptide vector as a carrier. Nucleic Acids Research, 27, 3510–3517.
Morris, M. C., Depollier, J., Mery, J., Heitz, F., & Divita, G. (2001). A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nature Biotechnology, 19, 1173–1176.
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. (2007). 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.
Moulay, G., Leborgne, C., Mason, A. J., Aisenbrey, C., Kichler, A., & Bechinger, B. (2017). Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multitude of cargo. Journal of Peptide Science, 23, 320–328.
Mukai, Y., Sugita, T., Yamato, T., Yamanada, N., Shibata, H., Imai, S., et al. (2006). Creation of novel Protein Transduction Domain (PTD) mutants by a phage display-based high-throughput screening system. Biological & Pharmaceutical Bulletin, 29, 1570–1574.
Munoz-Alarcon, A., Eriksson, J., & Langel, U. (2015). Novel efficient cell-penetrating, peptide-mediated strategy for enhancing telomerase inhibitor oligonucleotides. Nucleic Acid Therapeutics, 25, 306–310.
Murata, Y., Jo, J. I., & Tabata, Y. (2017). Preparation of gelatin nanospheres incorporating quantum dots and iron oxide nanoparticles for multimodal cell imaging. Journal of Biomaterials Science, Polymer Edition, 28, 555–568.
Muratovska, A., & Eccles, M. R. (2004). Conjugate for efficient delivery of short interfering RNA (siRNA) into mammalian cells. FEBS Letters, 558, 63–68.
Muthukrishnan, N., Donovan, S., & Pellois, J. P. (2014). The photolytic activity of poly-arginine cell penetrating peptides conjugated to carboxy-tetramethylrhodamine is modulated by arginine residue content and fluorophore conjugation site. Photochemistry and Photobiology, 90, 1034–1042.
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.
Nagel, Y. A., Raschle, P. S., & Wennemers, H. (2017). Effect of preorganized charge-display on the cell-penetrating properties of cationic peptides. Angewandte Chemie (International edition in English), 56, 122–126.
Najjar, K., Erazo-Oliveras, A., & Pellois, J. P. (2015). Delivery of proteins, peptides or cell-impermeable small molecules into live cells by incubation with the endosomolytic reagent dfTAT. Journal of Visualized Experiments, 2, 53175.
Nakamura, Y., Kogure, K., Futaki, S., & Harashima, H. (2007). Octaarginine-modified multifunctional envelope-type nano device for siRNA. Journal of Controlled Release, 119, 360–367.
Nakase, I., Akita, H., Kogure, K., Gräslund, A., Langel, Ü., Harashima, H., et al. (2012). Efficient intracellular delivery of nucleic acid pharmaceuticals using cell-penetrating peptides. Accounts of Chemical Research, 45, 1132–1139.
Nascimento, F. D., Hayashi, M. A., Kerkis, A., Oliveira, V., Oliveira, E. B., Radis-Baptista, G., et al. (2007). Crotamine mediates gene delivery into cells through the binding to heparan sulfate proteoglycans. Journal of Biological Chemistry, 282, 21349–21360.
Ndeboko, B., Ramamurthy, N., Lemamy, G. J., Jamard, C., Nielsen, P. E., & Cova, L. (2017). Role of cell-penetrating peptides in intracellular delivery of peptide nucleic acids targeting hepadnaviral replication. Molecular Therapy—Nucleic Acids, 9, 162–169.
Neundorf, I. (2017). Metal complex-peptide conjugates: How to modulate bioactivity of metal-containing compounds by the attachment to peptides. Current Medicinal Chemistry, 24, 1853–1861.
Ni, Z., Gong, Y., Dai, X., Ding, W., Wang, B., Gong, H., et al. (2015). AU4S: a novel synthetic peptide to measure the activity of ATG4 in living cells. Autophagy, 11, 403–415.
Niidome, T., Urakawa, M., Takaji, K., Matsuo, Y., Ohmori, N., Wada, A., et al. (1999). Influence of lipophilic groups in cationic alpha-helical peptides on their abilities to bind with DNA and deliver genes into cells. Journal of Peptide Research, 54, 361–367.
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.
Noguchi, H., Bonner-Weir, S., Wei, F. Y., Matsushita, M., & Matsumoto, S. (2005). BETA2/NeuroD protein can be transduced into cells due to an arginine- and lysine-rich sequence. Diabetes, 54, 2859–2866.
Noguchi, H., Kaneto, H., Weir, G. C., & Bonner-Weir, S. (2003). PDX-1 protein containing its own antennapedia-like protein transduction domain can transduce pancreatic duct and islet cells. Diabetes, 52, 1732–1737.
Nussbaumer, M. G., Duskey, J. T., Rother, M., Renggli, K., Chami, M., & Bruns, N. (2016). Chaperonin-Dendrimer conjugates for siRNA Delivery. Advanced science (Weinheim, Baden-Wurttemberg, Germany), 3, 1600046.
O’Connor, R. M., Gururajan, A., Dinan, T. G., Kenny, P. J., & Cryan, J. F. (2016). All Roads Lead to the miRNome: miRNAs Have a Central Role in the Molecular Pathophysiology of Psychiatric Disorders. Trends in Pharmacological Sciences, 37, 1029–1044.
Oh, S. Y., Ju, Y., Kim, S., & Park, H. (2010). PNA-based antisense oligonucleotides for micrornas inhibition in the absence of a transfection reagent. Oligonucleotides, 20, 225–230.
Oh, S. Y., Ju, Y., & Park, H. (2009). A highly effective and long-lasting inhibition of miRNAs with PNA-based antisense oligonucleotides. Molecules and Cells, 28, 341–345.
Okuda-Shinagawa, N. M., Moskalenko, Y. E., Junqueira, H. C., Baptista, M. S., Marques, C. M., & Machini, M. T. (2017). Fluorescent and photosensitizing conjugates of cell-penetrating peptide TAT(47-57): Design, microwave-assisted synthesis at 60 °C, and properties. ACS Omega, 2, 8156–8166.
O’malley, W. I., Rubbiani, R., Aulsebrook, M. L., Grace, M. R., Spiccia, L., Tuck, K. L., et al. (2016). Cellular uptake and photo-cytotoxicity of a Gadolinium(III)-DOTA-Naphthalimide complex “clicked” to a lipidated tat peptide. Molecules, 21.
Onoshima, D., Yukawa, H., & Baba, Y. (2015). Multifunctional quantum dots-based cancer diagnostics and stem cell therapeutics for regenerative medicine. Advanced Drug Delivery Reviews, 95, 2–14.
Oskolkov, N., Arukuusk, P., Copolovici, D.-M., Lindberg, S., Margus, H., Padari, K., et al. (2011). NickFects, phosphorylated derivatives of transportan 10 for cellular delivery of oligonucleotides. International Journal of Peptide Research and Therapeutics, 17, 147–157.
Östlund, P., Kilk, K., Lindgren, M., Hällbrink, M., Jiang, Y., Budihna, M., et al. (2005). Cell-penetrating mimics of agonist-activated G-protein coupled receptors. International Journal of Peptide Research and Therapeutics, 11, 237–247.
Paasonen, L., Sharma, S., Braun, G. B., Kotamraju, V. R., Chung, T. D., She, Z. G., et al. (2016). New p32/gC1qR ligands for targeted tumor drug delivery. ChemBioChem, 17, 570–575.
Padari, K., Koppel, K., Lorents, A., Hallbrink, M., Mano, M., Pedroso De Lima, M. C., et al. (2010). S4(13)-PV cell-penetrating peptide forms nanoparticle-like structures to gain entry into cells. Bioconjugate Chemistry, 21, 774–783.
Pan, D., Hu, Z., Qiu, F., Huang, Z. L., Ma, Y., Wang, Y., et al. (2014). A general strategy for developing cell-permeable photo-modulatable organic fluorescent probes for live-cell super-resolution imaging. Nature Communications, 5, 5573.
Pärn, K., Viru, L., Lehto, T., Oskolkov, N., Langel, Ü., & Merits, A. (2013). Transfection of infectious RNA and DNA/RNA layered vectors of semliki forest virus by the cell-penetrating peptide based reagent PepFect6. PLoS ONE, 8, e69659.
Pärnaste, L., Arukuusk, P., Langel, K., Tenson, T., & Langel, Ü. (2017). The formation of nanoparticles between small interfering RNA and amphipathic cell-penetrating peptides. Molecular Therapy—Nucleic Acids, 7, 1–10.
Parsons, K. H., Mondal, M. H., McCormick, C. L., & Flynt, A. S. (2018). Guanidinium-functionalized interpolyelectrolyte complexes enabling RNAi in resistant insect pests. Biomacromolecules.
Pazos, I. M., Ahmed, I. A., Berrios, M. I., & Gai, F. (2015). Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics. Analytical Biochemistry, 483, 21–26.
Peitz, M., Munst, B., Thummer, R. P., Helfen, M., & Edenhofer, F. (2014). Cell-permeant recombinant Nanog protein promotes pluripotency by inhibiting endodermal specification. Stem Cell Research, 12, 680–689.
Peng, J., Rao, Y., Yang, X., Jia, J., Wu, Y., Lu, J., et al. (2017a). Targeting neuronal nitric oxide synthase by a cell penetrating peptide Tat-LK15/siRNA bioconjugate. Neuroscience Letters, 650, 153–160.
Peng, F., Tu, Y., Adhikari, A., Hintzen, J. C., Lowik, D. W., & Wilson, D. A. (2017b). A peptide functionalized nanomotor as an efficient cell penetrating tool. Chemical Communications (Cambridge, England), 53, 1088–1091.
Peraro, L., & Kritzer, J. (2018). Getting in: Emerging methods and design principles for cell-penetrant peptides. Angewandte Chemie International Edition in English.
Peritz, T., Zeng, F., Kannanayakal, T. J., Kilk, K., Eiriksdottir, E., Langel, Ü., et al. (2006). Immunoprecipitation of mRNA-protein complexes. Nature Protocols, 1, 577–580.
Pham, W., Kircher, M. F., Weissleder, R., & Tung, C. H. (2004). Enhancing membrane permeability by fatty acylation of oligoarginine peptides. ChemBioChem, 5, 1148–1151.
Poillot, C., Bichraoui, H., Tisseyre, C., Bahemberae, E., Andreotti, N., Sabatier, J. M., et al. (2012). Small efficient cell-penetrating peptides derived from scorpion toxin maurocalcine. Journal of Biological Chemistry, 287, 17331–17342.
Polyakov, V., Sharma, V., Dahlheimer, J. L., Pica, C. M., Luker, G. D., & Piwnica-Worms, D. (2000). Novel Tat-peptide chelates for direct transduction of technetium-99 m and rhenium into human cells for imaging and radiotherapy. Bioconjugate Chemistry, 11, 762–771.
Pooga, M., Hällbrink, M., Zorko, M., & Langel, Ü. (1998a). Cell penetration by transportan. FASEB Journal, 12, 67–77.
Pooga, M., Jureus, A., Razaei, K., Hasanvan, H., Saar, K., Kask, K., et al. (1998b). Novel galanin receptor ligands. Journal of Peptide Research, 51, 65–74.
Pooga, M., Land, T., Bartfai, T., & Langel, Ü. (2001). PNA oligomers as tools for specific modulation of gene expression. Biomolecular Engineering, 17, 183–192.
Pooga, M., Soomets, U., Hällbrink, M., Valkna, A., Saar, K., Rezaei, K., et al. (1998c). Cell penetrating PNA constructs regulate galanin receptor levels and modify pain transmission in vivo. Nature Biotechnology, 16, 857–861.
Poutiainen, P. K., Ronkko, T., Hinkkanen, A. E., Palvimo, J. J., Narvanen, A., Turhanen, P., et al. (2014). Firefly luciferase inhibitor-conjugated peptide quenches bioluminescence: A versatile tool for real time monitoring cellular uptake of biomolecules. Bioconjugate Chemistry, 25, 4–10.
Prantner, A. M., Sharma, V., Garbow, J. R., & Piwnica-Worms, D. (2003). Synthesis and characterization of a Gd-DOTA-D-permeation peptide for magnetic resonance relaxation enhancement of intracellular targets. Molecular Imaging, 2, 333–341.
Przysiecka, L., Michalska, M., Nowaczyk, G., Peplinska, B., Jesionowski, T., Schneider, R., et al. (2016). iRGD peptide as effective transporter of CuInZnxS2 + x quantum dots into human cancer cells. Colloids and Surfaces B: Biointerfaces, 146, 9–18.
Pushpanathan, M., Gunasekaran, P., & Rajendhran, J. (2013). Mechanisms of the antifungal action of marine metagenome-derived peptide, MMGP1, against Candida albicans. PLoS One, 8.
Quinn, M. K., Gnan, N., James, S., Ninarello, A., Sciortino, F., Zaccarelli, E., et al. (2015). How fluorescent labelling alters the solution behaviour of proteins. Physical Chemistry Chemical Physics: PCCP, 17, 31177–31187.
Radis-Baptista, G., Campelo, I. S., Morlighem, J. R. L., Melo, L. M., & Freitas, V. J. F. (2017). Cell-penetrating peptides (CPPs): From delivery of nucleic acids and antigens to transduction of engineered nucleases for application in transgenesis. Journal of Biotechnology, 4, 30203-1.
Radwani, H., Lopez-Gonzalez, M. J., Cattaert, D., Roca-Lapirot, O., Dobremez, E., Bouali-Benazzouz, R., et al. (2016). Cav1.2 and Cav1.3 L-type calcium channels independently control short- and long-term sensitization to pain. The Journal of Physiology, 594, 6607–6626.
Rajendran, M., Yapici, E., & Miller, L. W. (2014). Lanthanide-based imaging of protein-protein interactions in live cells. Inorganic Chemistry, 53, 1839–1853.
Ramaker, K., Henkel, M., Krause, T., Rockendorf, N., & Frey, A. (2018). Cell penetrating peptides: A comparative transport analysis for 474 sequence motifs. Drug Delivery, 25, 928–937.
Ramakrishna, S., Kwaku Dad, A. B., Beloor, J., Gopalappa, R., Lee, S. K., & Kim, H. (2014). Gene disruption by cell-penetrating peptide-mediated delivery of Cas9 protein and guide RNA. Genome Resarch, 24, 1020–1027.
Rathnayake, P. V., Gunathunge, B. G., Wimalasiri, P. N., Karunaratne, D. N., & Ranatunga, R. J. (2017). Trends in the binding of cell penetrating peptides to siRNA: A molecular docking study. J Biophys, 2017, 1059216.
Regberg, J., Srimanee, A., Erlandsson, M., Sillard, R., Dobchev, D. A., Karelson, M., et al. (2014). Rational design of a series of novel amphipathic cell-penetrating peptides. International Journal of Pharmaceutics, 464, 111–116.
Regberg, J., Vasconcelos, L., Madani, F., Langel, Ü., & Hällbrink, M. (2016). pH-responsive PepFect cell-penetrating peptides. International Journal of Pharmaceutics, 501, 32–38.
Rittner, K., Benavente, A., Bompard-Sorlet, A., Heitz, F., Divita, G., Brasseur, R., et al. (2002). New basic membrane-destabilizing peptides for plasmid-based gene delivery in vitro and in vivo. Molecular Therapy, 5, 104–114.
Roberts, T. C., Ezzat, K., el Andaloussi, S., & Weinberg, M. S. (2016). Synthetic SiRNA delivery: Progress and prospects. Methods in Molecular Biology, 1364, 291–310.
Rodrigues, M., Santos, A., de la Torre, B. G., Radis-Baptista, G., Andreu, D., & Santos, N. C. (2012). Molecular characterization of the interaction of crotamine-derived nucleolar targeting peptides with lipid membranes. Biochimica et Biophysica Acta, 1818, 2707–2717.
Ross, K. (2018). Towards topical microRNA-directed therapy for epidermal disorders. Journal of Controlled Release, 269, 136–147.
Roth, L., Agemy, L., Kotamraju, V. R., Braun, G., Teesalu, T., Sugahara, K. N., et al. (2012). Transtumoral targeting enabled by a novel neuropilin-binding peptide. Oncogene, 31, 3754–3763.
Roux, L. N., Petit, I., Domart, R., Concordet, J. P., Qu, J., Zhou, H., et al. (2018). Modeling of Aniridia-related keratopathy by CRISPR/Cas9 genome editing of human limbal epithelial cells and rescue by recombinant PAX6 protein. Stem Cells.
Ru, R., Yao, Y., Yu, S., Yin, B., Xu, W., Zhao, S., et al. (2013). Targeted genome engineering in human induced pluripotent stem cells by penetrating TALENs. Cell Regeneration (London), 2, 5.
Ruan, G., Agrawal, A., Marcus, A. I., & Nie, S. (2007). Imaging and tracking of tat peptide-conjugated quantum dots in living cells: new insights into nanoparticle uptake, intracellular transport, and vesicle shedding. Journal of the American Chemical Society, 129, 14759–14766.
Rudolph, C., Plank, C., Lausier, J., Schillinger, U., Müller, R. H., & Rosenecker, J. (2003). Oligomers of the arginine-rich motif of the HIV-1 TAT protein are capable of transferring plasmid DNA into cells. Journal of Biological Chemistry, 278, 11411–11418.
Ryu, J. H., Lee, A., Na, J. H., Lee, S., Ahn, H. J., Park, J. W., et al. (2011). Optimization of matrix metalloproteinase fluorogenic probes for osteoarthritis imaging. Amino Acids, 41, 1113–1122.
Säälik, P., Elmquist, A., Hansen, M., Padari, K., Saar, K., Viht, K., et al. (2004). Protein cargo delivery properties of cell-penetrating peptides. A comparative study. Bioconjugate Chemistry, 15, 1246–1253.
Sakurai, Y., Hatakeyama, H., Sato, Y., Akita, H., Takayama, K., Kobayashi, S., et al. (2011). Endosomal escape and the knockdown efficiency of liposomal-siRNA by the fusogenic peptide shGALA. Biomaterials, 32, 5733–5742.
Saleh, T., Bolhassani, A., Shojaosadati, S. A., & Aghasadeghi, M. R. (2015). MPG-based nanoparticle: An efficient delivery system for enhancing the potency of DNA vaccine expressing HPV16E7. Vaccine, 33, 3164–3170.
Salerno, J. C., Ngwa, V. M., Nowak, S. J., Chrestensen, C. A., Healey, A. N., & McMurry, J. L. (2016). Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos. Journal of Cell Science, 129, 893–897.
Salzano, G., Costa, D. F., Sarisozen, C., Luther, E., Mattheolabakis, G., Dhargalkar, P. P., et al. (2016). Mixed nanosized polymeric micelles as promoter of doxorubicin and miRNA-34a co-delivery triggered by dual stimuli in tumor tissue. Small (Weinheim an der Bergstrasse, Germany), 12, 4837–4848.
Sandberg, M., Eriksson, L., Jonsson, J., Sjostrom, M., & Wold, S. (1998). New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids. Journal of Medicinal Chemistry, 41, 2481–2491.
Sanders, W. S., Johnston, C. I., Bridges, S. M., Burgess, S. C., & Willeford, K. O. (2011). Prediction of cell penetrating peptides by support vector machines. PLoS Computational Biology, 7, e1002101.
Sangtani, A., Petryayeva, E., Wu, M., Susumu, K., Oh, E., Huston, A. L., et al. (2018). Intracellularly actuated quantum dot-peptide-doxorubicin nanobioconjugates for controlled drug delivery via the endocytic pathway. Bioconjugate Chemistry, 29, 136–148.
Saw, P. E., Ko, Y. T., & Jon, S. (2010). Efficient liposomal nanocarrier-mediated oligodeoxynucleotide delivery involving dual use of a cell-penetrating peptide as a packaging and intracellular delivery agent. Macromolecular Rapid Communications, 31, 1155–1162.
Sayers, E. J., Cleal, K., Eissa, N. G., Watson, P., & Jones, A. T. (2014). Distal phenylalanine modification for enhancing cellular delivery of fluorophores, proteins and quantum dots by cell penetrating peptides. Journal of Controlled Release, 195, 55–62.
Sazani, P., Gemignani, F., Kang, S. H., Maier, M. A., Manoharan, M., Persmark, M., et al. (2002). Systemically delivered antisense oligomers upregulate gene expression in mouse tissues. Nature Biotechnology, 20, 1228–1233.
Sazani, P., Kang, S. H., Maier, M. A., Wei, C., Dillman, J., Summerton, J., et al. (2001). Nuclear antisense effects of neutral, anionic and cationic oligonucleotide analogs. Nucleic Acids Research, 29, 3965–3974.
Scarfi, S., Giovine, M., Gasparini, A., Damonte, G., Millo, E., Pozzolini, M., et al. (1999). Modified peptide nucleic acids are internalized in mouse macrophages RAW 264.7 and inhibit inducible nitric oxide synthase. FEBS Letters, 451, 264–268.
Schmidt, S., Adjobo-Hermans, M. J., Kohze, R., Enderle, T., Brock, R., & Milletti, F. (2017). Identification of short hydrophobic cell-penetrating peptides for cytosolic peptide delivery by rational design. Bioconjugate Chemistry, 28, 382–389.
Schnittert, J., Kuninty, P. R., Bystry, T. F., Brock, R., Storm, G., & Prakash, J. (2017). Anti-microRNA targeting using peptide-based nanocomplexes to inhibit differentiation of human pancreatic stellate cells. Nanomedicine (London).
Sciani, J. M., Vigerelli, H., Costa, A. S., Camara, D. A., Junior, P. L., & Pimenta, D. C. (2017). An unexpected cell-penetrating peptide from Bothrops jararaca venom identified through a novel size exclusion chromatography screening. Journal of Peptide Science, 23, 68–76.
Segura, J., Fillat, C., Andreu, D., Llop, J., Millan, O., de la Torre, B. G., et al. (2007). Monitoring gene therapy by external imaging of mRNA: Pilot study on murine erythropoietin. Therapeutic Drug Monitoring, 29, 612–618.
Seo, B. J., Hong, Y. J., & Do, J. T. (2017). Cellular reprogramming using protein and cell-penetrating peptides. International Journal of Molecular Sciences, 18.
Shiraishi, T., & Nielsen, P. E. (2011). Peptide nucleic acid (PNA) cell penetrating peptide (CPP) conjugates as carriers for cellular delivery of antisense oligomers. Artif DNA PNA XNA, 2, 90–99.
Shukla, R. S., Qin, B., & Cheng, K. (2014). Peptides used in the delivery of small noncoding RNA. Molecular Pharmaceutics, 11, 3395–3408.
Simeoni, F., Morris, M. C., Heitz, F., & Divita, G. (2003). Insight into the mechanism of the peptide-based gene delivery system MPG: Implications for delivery of siRNA into mammalian cells. Nucleic Acids Research, 31, 2717–2724.
Simmons, C. G., Pitts, A. E., Mayfield, L. D., Shay, J. W., & Corey, D. R. (1997). Synthesis and membrane permeability of PNA-peptide conjugates. Bioorganic & Medicinal Chemistry Letters, 7, 3001–3006.
Song, J., Kai, M., Zhang, W., Zhang, J., Liu, L., Zhang, B., et al. (2011). Cellular uptake of transportan 10 and its analogs in live cells: Selectivity and structure-activity relationship studies. Peptides, 32, 1934–1941.
Song, L., Liang, X., Yang, S., Wang, N., He, T., Wang, Y., et al. (2018). Novel polyethyleneimine-R8-heparin nanogel for high-efficiency gene delivery in vitro and in vivo. Drug Delivery, 25, 122–131.
Soomets, U., Hällbrink, M., Zorko, M., & Langel, Ü. (1997). From galanin and mastoparan to galparan and transportan. Current Topics in Peptide and Protein Res., 2, 83–113.
Soudah, T., Mogilevsky, M., Karni, R., & Yavin, E. (2017). CLIP6-PNA-Peptide conjugates: Non-endosomal delivery of splice switching oligonucleotides. Bioconjugate Chemistry, 28, 3036–3042.
Sousa, A. A., Morgan, J. T., Brown, P. H., Adams, A., Jayasekara, M. P., Zhang, G., et al. (2012). Synthesis, characterization, and direct intracellular imaging of ultrasmall and uniform glutathione-coated gold nanoparticles. Small (Weinheim an der Bergstrasse, Germany), 8, 2277–2286.
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. International Journal of Peptide Research and Therapeutics, 20, 169–178.
Stein, C. A., & Castanotto, D. (2017). FDA-approved oligonucleotide therapies in 2017. Molecular Therapy, 25, 1069–1075.
Suchaoin, W., Mahmood, A., Netsomboon, K., & Bernkop-Schnurch, A. (2017). Zeta-potential-changing nanoparticles conjugated with cell-penetrating peptides for enhanced transfection efficiency. Nanomedicine (London), 12, 963–975.
Sugahara, K. N., Braun, G. B., de Mendoza, T. H., Kotamraju, V. R., French, R. P., Lowy, A. M., et al. (2015). Tumor-penetrating iRGD peptide inhibits metastasis. Molecular Cancer Therapeutics, 14, 120–128.
Suh, J. S., Lee, J. Y., Choi, Y. S., Chung, C. P., & Park, Y. J. (2013). Peptide-mediated intracellular delivery of miRNA-29b for osteogenic stem cell differentiation. Biomaterials, 34, 4347–4359.
Suh, J. S., Lee, J. Y., Choi, Y. J., You, H. K., Hong, S. D., Chung, C. P., et al. (2014a). Intracellular delivery of cell-penetrating peptide-transcriptional factor fusion protein and its role in selective osteogenesis. International Journal of Nanomedicine, 9, 1153–1166.
Suh, J. S., Lee, J. Y., Lee, G., Chung, C. P., & Park, Y. J. (2014b). Simultaneous imaging and restoration of cell function using cell permeable peptide probe. Biomaterials, 35, 6287–6298.
Suresh, B., Ramakrishna, S., & Kim, H. (2017). Cell-penetrating peptide-mediated delivery of Cas9 protein and guide RNA for genome editing. Methods in Molecular Biology, 81–94.
Suryawanshi, H., Sarangdhar, M. A., Vij, M., Roshan, R., Singh, V. P., Ganguli, M., et al. (2015). A simple alternative to stereotactic injection for brain specific knockdown of miRNA. Journal of Visualized Experiments, 26, 53307.
Swiecicki, J. M., di Pisa, M., Burlina, F., Lecorche, P., Mansuy, C., Chassaing, G., et al. (2015). Accumulation of cell-penetrating peptides in large unilamellar vesicles: A straightforward screening assay for investigating the internalization mechanism. Biopolymers, 104, 533–543.
Tai, W., & Gao, X. (2016). Functional peptides for siRNA delivery. Advanced Drug Delivery Reviews, 13, 30236–30238.
Takahashi, K., & Yamanaka, S. (2006). Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell, 126, 663–676.
Takashina, T., Koyama, T., Nohara, S., Hasegawa, M., Ishiguro, A., Iijima, K., et al. (2018). Identification of a cell-penetrating peptide applicable to a protein-based transcription activator-like effector expression system for cell engineering. Biomaterials, 173, 11–21.
Tang, H., Su, Z. D., Wei, H. H., Chen, W., & Lin, H. (2016). Prediction of cell-penetrating peptides with feature selection techniques. Biochemical and Biophysical Research Communications, 477, 150–154.
Teesalu, T., Sugahara, K. N., & Ruoslahti, E. (2013). Tumor-penetrating peptides. Frontiers in Oncology, 3.
Theunissen, T. W., Costa, Y., Radzisheuskaya, A., van Oosten, A. L., Lavial, F., Pain, B., et al. (2011). Reprogramming capacity of Nanog is functionally conserved in vertebrates and resides in a unique homeodomain. Development, 138, 4853–4865.
Thiagarajan, L., Abu-Awwad, H. A. M., & Dixon, J. E. (2017). Osteogenic programming of human mesenchymal stem cells with highly efficient intracellular delivery of RUNX2. Stem Cells Translational Medicine, 6, 2146–2159.
Thierry, A. R., Abes, S., Resina, S., Travo, A., Richard, J. P., Prevot, P., et al. (2006). Comparison of basic peptides- and lipid-based strategies for the delivery of splice correcting oligonucleotides. Biochimica et Biophysica Acta, 1758, 364–374.
Thoren, P. E., Persson, D., Esbjorner, E. K., Goksor, M., Lincoln, P., & Norden, B. (2004). Membrane binding and translocation of cell-penetrating peptides. Biochemistry, 43, 3471–3489.
Tisseyre, C., Ahmadi, M., Bacot, S., Dardevet, L., Perret, P., Ronjat, M., et al. (2014). Quantitative evaluation of the cell penetrating properties of an iodinated Tyr-l-maurocalcine analog. Biochimica et Biophysica Acta, 1843, 2356–2364.
Torres, A. G., Fabani, M. M., Vigorito, E., Williams, D., Al-Obaidi, N., Wojciechowski, F., et al. (2012). Chemical structure requirements and cellular targeting of microRNA-122 by peptide nucleic acids anti-miRs. Nucleic Acids Research, 40, 2152–2167.
Tung, C. H., Mueller, S., & Weissleder, R. (2002). Novel branching membrane translocational peptide as gene delivery vector. Bioorganic & Medicinal Chemistry, 10, 3609–3614.
Tuttolomondo, M., Casella, C., Hansen, P. L., Polo, E., Herda, L. M., Dawson, K. A., et al. (2017). Human DMBT1-Derived cell-penetrating peptides for intracellular siRNA delivery. Molecular Therapy—Nucleic Acids, 8, 264–276.
Udhayakumar, V. K., De Beuckelaer, A., McCaffrey, J., McCrudden, C. M., Kirschman, J. L., Vanover, D., et al. (2017). Arginine-rich peptide-based mRNA nanocomplexes efficiently instigate cytotoxic T cell immunity dependent on the amphipathic organization of the peptide. Advanced Healthcare Materials, 6.
Upadhya, A., & Sangave, P. C. (2016). Hydrophobic and electrostatic interactions between cell penetrating peptides and plasmid DNA are important for stable non-covalent complexation and intracellular delivery. Journal of Peptide Science, 22, 647–659.
Urgard, E., Brjalin, A., Langel, U., Pooga, M., Rebane, A., & Annilo, T. (2017). Comparison of peptide- and lipid-based delivery of miR-34a-5p Mimic into PPC-1 cells. Nucleic Acid Therapeutics, 27, 295–302.
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.
Vaissiere, A., Aldrian, G., Konate, K., Lindberg, M. F., Jourdan, C., Telmar, A., et al. (2017). A retro-inverso cell-penetrating peptide for siRNA delivery. Journal of Nanobiotechnology, 15, 34.
van Asbeck, A. H., Beyerle, A., McNeill, H., Bovee-Geurts, P. H., Lindberg, S., Verdurmen, W. P., et al. (2013). Molecular parameters of siRNA–cell penetrating peptide nanocomplexes for efficient cellular delivery. ACS Nano, 7, 3797–3807.
van den Berg, A., & Dowdy, S. F. (2011). Protein transduction domain delivery of therapeutic macromolecules. Current Opinion in Biotechnology, 22, 888–893.
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.
Vij, M., Natarajan, P., Pattnaik, B. R., Alam, S., Gupta, N., Santhiya, D., et al. (2016). Non-invasive topical delivery of plasmid DNA to the skin using a peptide carrier. Journal of Controlled Release, 222, 159–168.
Wada, S. I., Takesada, A., Nagamura, Y., Sogabe, E., Ohki, R., Hayashi, J., et al. (2017). Structure-activity relationship study of Aib-containing amphipathic helical peptide-cyclic RGD conjugates as carriers for siRNA delivery. Bioorganic & Medicinal Chemistry Letters, 27, 5378–5381.
Wan, Y., Moyle, P. M., Christie, M. P., & Toth, I. (2016). Nanosized, peptide-based multicomponent DNA delivery systems: Optimization of endosome escape activity. Nanomedicine (London), 11, 907–919.
Wan, Y., Moyle, P. M., Gn, P. Z., & Toth, I. (2017). Design and evaluation of a stearylated multicomponent peptide-siRNA nanocomplex for efficient cellular siRNA delivery. Nanomedicine (London), 12, 281–293.
Wang, X., & Jauch, R. (2014). OCT4: A penetrant pluripotency inducer. Cell Regeneration (London), 3, 6.
Wang, H. X., Song, Z., Lao, Y. H., Xu, X., Gong, J., Cheng, D., et al. (2018a). Nonviral gene editing via CRISPR/Cas9 delivery by membrane-disruptive and endosomolytic helical polypeptide. Proceedings of the National Academy of Sciences USA, 115, 4903–4908.
Wang, L., Tang, W., Yan, S., Zhou, L., Shen, T., Huang, X., et al. (2013). Efficient delivery of miR-122 to regulate cholesterol metabolism using a non-covalent peptide-based strategy. Molecular Medicine Reports, 8, 1472–1478.
Wang, X., Wu, F., Li, G., Zhang, N., Song, X., Zheng, Y., et al. (2018b). Lipid-modified cell-penetrating peptide-based self-assembly micelles for co-delivery of narciclasine and siULK1 in hepatocellular carcinoma therapy. Acta Biomaterialia.
Wei, L., Tang, J., & Zou, Q. (2017a). SkipCPP-Pred: An improved and promising sequence-based predictor for predicting cell-penetrating peptides. BMC Genomics, 18, 742.
Wei, L., Xing, P., Su, R., Shi, G., Ma, Z. S., & Zou, Q. (2017b). CPPred-RF: A sequence-based predictor for identifying cell-penetrating peptides and their uptake efficiency. Journal of Proteome Research, 16, 2044–2053.
Weiss, H. M., Wirz, B., Schweitzer, A., Amstutz, R., Rodriguez Perez, M. I., Andres, H., et al. (2007). ADME investigations of unnatural peptides: distribution of a 14C-labeled beta 3-octaarginine in rats. Chemistry & Biodiversity, 4, 1413–1437.
Willmore, A. A., Simon-Gracia, L., Toome, K., Paiste, P., Kotamraju, V. R., Molder, T., et al. (2015). Targeted silver nanoparticles for ratiometric cell phenotyping. Nanoscale, 8, 8.
Wolfe, J. M., Fadzen, C. M., Choo, Z. N., Holden, R. L., Yao, M., Hanson, G. J., et al. (2018a). Machine learning to predict cell-penetrating peptides for antisense delivery. ACS Central Science, 4, 512–520.
Wolfe, J. M., Fadzen, C. M., Holden, R. L., Yao, M., Hanson, G. J., & Pentelute, B. L. (2018b). Perfluoroaryl bicyclic cell-penetrating peptides for delivery of antisense oligonucleotides. Angewandte Chemie International Edition in English.
Wu, Y., Sun, J., Li, A., & Chen, D. (2018). The promoted delivery of RRM2 siRNA to vascular smooth muscle cells through liposome-polycation-DNA complex conjugated with cell penetrating peptides. Biomedicine & Pharmacotherapy, 103, 982–988.
Wyman, T. B., Nicol, F., Zelphati, O., Scaria, P. V., Plank, C., & Szoka Jr., F. C. (1997). Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers. Biochemistry, 36, 3008–3017.
Xia, M. C., Cai, L., Zhang, S., & Zhang, X. (2018). A cell-penetrating ratiometric probe for simultaneous measurement of lysosomal and cytosolic pH change. Talanta, 178, 355–361.
Xie, X., Lin, W., Li, M., Yang, Y., Deng, J., Liu, H., et al. (2016). Efficient siRNA delivery using novel cell-penetrating peptide-siRNA conjugate-loaded nanobubbles and ultrasound. Ultrasound in Medicine and Biology, 42, 1362–1374.
Xu, H., Bao, X., Wang, Y., Xu, Y., Deng, B., Lu, Y., et al. (2018). Engineering T7 bacteriophage as a potential DNA vaccine targeting delivery vector. Virology Journal, 15, 49.
Xu, J., Xiang, Q., Su, J., Yang, P., Zhang, Q., Su, Z., et al. (2014). Evaluation of the safety and brain-related tissues distribution characteristics of TAT-HaFGF via intranasal administration. Biological & Pharmaceutical Bulletin, 37, 1149–1157.
Xue, X. Y., Mao, X. G., Zhou, Y., Chen, Z., Hu, Y., Hou, Z., et al. (2018). Advances in the delivery of antisense oligonucleotides for combating bacterial infectious diseases. Nanomedicine (Lond), 14, 745–758.
Yamaguchi, S., Ito, S., Kurogi-Hirayama, M., & Ohtsuki, S. (2017). Identification of cyclic peptides for facilitation of transcellular transport of phages across intestinal epithelium in vitro and in vivo. Journal of Controlled Release, 262, 232–238.
Yang, Y., Xia, X., Dong, W., Wang, H., Li, L., Ma, P., et al. (2016a). Acid sensitive polymeric micelles combining folate and bioreducible conjugate for specific intracellular siRNA delivery. Macromolecular Bioscience, 16, 759–773.
Yang, Y., Xie, X., Xu, X., Xia, X., Wang, H., Li, L., et al. (2016b). Thermal and magnetic dual-responsive liposomes with a cell-penetrating peptide-siRNA conjugate for enhanced and targeted cancer therapy. Colloids Surf B Biointerfaces, 146, 607–615.
Yang, Y., Yang, Y., Xie, X., Xu, X., Xia, X., Wang, H., et al. (2016c). Dual stimulus of hyperthermia and intracellular redox environment triggered release of siRNA for tumor-specific therapy. International Journal of Pharmaceutics, 506, 158–173.
Yao, H., Wang, K., Wang, Y., Wang, S., Li, J., Lou, J., et al. (2015). Enhanced blood-brain barrier penetration and glioma therapy mediated by a new peptide modified gene delivery system. Biomaterials, 37, 345–352.
Ye, J., Liu, E., Gong, J., Wang, J., Huang, Y., He, H., et al. (2017). High-yield synthesis of monomeric LMWP(CPP)-siRNA covalent conjugate for effective cytosolic delivery of siRNA. Theranostics, 7, 2495–2508.
Yong, K.-T. (2010). Biophotonics and biotechnology in pancreatic cancer: Cyclic RGD-peptide-conjugated Type II quantum dots for in vivo imaging. Pancreatology, 10, 553–564.
Yoo, J., Lee, D., Gujrati, V., Rejinold, N. S., Lekshmi, K. M., Uthaman, S., et al. (2017). Bioreducible branched poly(modified nona-arginine) cell-penetrating peptide as a novel gene delivery platform. Journal of Controlled Release, 246, 142–154.
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.
Yu, Z., Ye, J., Pei, X., Sun, L., Liu, E., Wang, J., et al. (2018). Improved method for synthesis of low molecular weight protamine-siRNA conjugate. Acta pharmaceutica Sinica. B, 8, 116–126.
Yukawa, H., Kagami, Y., Watanabe, M., Oishi, K., Miyamoto, Y., Okamoto, Y., et al. (2010a). Quantum dots labeling using octa-arginine peptides for imaging of adipose tissue-derived stem cells. Biomaterials, 31, 4094–4103.
Yukawa, H., Noguchi, H., Nakase, I., Miyamoto, Y., Oishi, K., Hamajima, N., et al. (2010b). Transduction of cell-penetrating peptides into induced pluripotent stem cells. Cell Transplantation, 19, 901–909.
Yukawa, H., Suzuki, K., Kano, Y., Yamada, T., Kaji, N., Ishikawa, T., et al. (2013). Induced pluripotent stem cell labeling using quantum dots. Cell Med, 6, 83–90.
Zamaleeva, A. I., Despras, G., Luccardini, C., Collot, M., de Waard, M., Oheim, M., et al. (2015). FRET-based nanobiosensors for imaging intracellular Ca(2)(+) and H(+) microdomains. Sensors (Basel), 15, 24662–24680.
Zeng, F., Peritz, T., Kannanayakal, T. J., Kilk, K., Eiriksdottir, E., Langel, Ü., et al. (2006). A protocol for PAIR: PNA-assisted identification of RNA binding proteins in living cells. Nature Protocols, 1, 920–927.
Zhang, L., Liang, D., Wang, Y., Li, D., Zhang, J., Wu, L., et al. (2018a). Caged circular siRNAs for photomodulation of gene expression in cells and mice. Chemical Science, 9, 44–51.
Zhang, Z., Yuan, Y., Liu, Z., Chen, H., Chen, D., Fang, X., et al. (2018b). Brightness enhancement of near-infrared semiconducting polymer dots for in vivo whole-body cell tracking in deep organs. ACS Applied Materials & Interfaces, 10, 26928–26935.
Zhang, M., Zhao, X., Geng, J., Liu, H., Zeng, F., Qin, Y., et al. (2018b). Efficient penetration of Scp01-b and its DNA transfer abilities into cells. Journal of Cell Physiology.
Zhang, L., Zhou, Q., Song, W., Wu, K., Zhang, Y., & Zhao, Y. (2017). Dual-functionalized graphene oxide based siRNA delivery system for implant surface biomodification with enhanced osteogenesis. ACS Applied Materials & Interfaces, 9, 34722–34735.
Zhao, Y., He, Z., Gao, H., Tang, H., He, J., Guo, Q., et al. (2018). Fine tuning of core-shell structure of hyaluronic acid/cell-penetrating peptides/siRNA nanoparticles for enhanced gene delivery to macrophages in antiatherosclerotic therapy. Biomacromolecules.
Zielinski, J., Kilk, K., Peritz, T., Kannanayakal, T., Miyashiro, K. Y., Eiriksdottir, E., et al. (2006). In vivo identification of ribonucleoprotein-RNA interactions. Proceedings of the National Academy of Sciences USA, 103, 1557–1562.
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.
Zuris, J. A., Thompson, D. B., Shu, Y., Guilinger, J. P., Bessen, J. L., Hu, J. H., et al. (2015). Cationic lipid-mediated delivery of proteins enables efficient protein-based genome editing in vitro and in vivo. Nature Biotechnology, 33, 73–80.
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Langel, Ü. (2019). Methods for CPP Functionalization. In: CPP, Cell-Penetrating Peptides. Springer, Singapore. https://doi.org/10.1007/978-981-13-8747-0_3
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