Abstract
L-asparaginase, a cancer therapeutic enzyme, has attracted a great deal of attention from the scientific community. Although it was adopted in the treatment of leukaemia decades ago, its clinical formulations need to be improved. Current asparaginase formulations are derived from the terrestrial microorganisms, Escherichia coli and Erwinia chrysanthemi that elicit severe side effects to the patient. Moreover, these forms of asparaginase have been observed with a short half-life in the blood circulation, thereby requiring frequent dosage of the drug. Altogether, this results in increasing the cost of the treatment with lower clinical efficacy. Therefore, considerable research has been prompted in the acquisition of alternative sources of asparaginase with improved biochemical properties. Among the different sources, the marine environment is sparsely explored for biological products and enzymes. Marine resources that encompass vast diversity are a treasure trove of novel natural products. This chapter features the potential of marine-derived L-asparaginase and underlines the milestone chronicles of events in its discovery and adoption in the treatment of acute lymphoblastic leukaemia. Further, the nanoformulation of L-asparaginase has also been discussed, and the importance of bioinspired nanocarriers and nanozymes in the development of cancer therapeutics has been highlighted.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Abuchowski A, Kazo GM, Verhoest CR Jr, Van Es T, Kafkewitz D, Nucci ML, Viau AT, Davis FF (1984) Cancer therapy with chemically modified enzymes. I. Antitumor properties of polyethylene glycol-asparaginase conjugates. Cancer Biochem Biophys 7(2):175–186
Agrawal S, Kango N (2019) Development and catalytic characterization of L-asparaginase nano-bioconjugates. Int J Biol Macromol 135:1142–1150
Agrawal S, Sharma I, Prajapati BP, Suryawanshi RK, Kango N (2018) Catalytic characteristics and application of L-asparaginase immobilized on aluminum oxide pellets. Int J Biol Macromol 114:504–511
Ahmadpour S, Hosseinimehr SJ (2018) PASylation as a powerful technology for improving the pharmacokinetic properties of biopharmaceuticals. Curr Drug Deliv 15(3):331–341
Aibani N, Khan TN, Callan B (2020) Liposome mimicking polymersomes; A comparative study of the merits of polymersomes in terms of formulation and stability. Int J Pharmac X 2:100040
Al-Dulimi AG, Al-Saffar AZ, Sulaiman GM, Khalil KA, Khashan KS, Al-Shmgani HS, Ahmed EM (2020) Immobilization of L-asparaginase on gold nanoparticles for novel drug delivery approach as anti-cancer agent against human breast carcinoma cells. J Mater Res Technol 9(6):15394–15411
Alrumman SA, Mostafa YS, Al-izran KA et al (2019) Production and Anticancer Activity of an L-asparaginase from Bacillus licheniformis Isolated from the Red Sea, Saudi Arabia. Sci Rep 9:1–14. https://doi.org/10.1038/s41598-019-40512-x
Ammon HL, Weber IT, Wlodawer A, Harrison RW, Gilliland GL, Murphy KC, Sjölin L, Roberts J (1988) Preliminary crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase. J Biol Chem 263(1):150–156
Amylon MD, Shuster J, Pullen J et al (1999) Intensive high-dose asparaginase consolidation improves survival for pediatric patients with T cell acute lymphoblastic leukemia and advanced stage lymphoblastic lymphoma: A Pediatric Oncology Group study. Leukemia 13:335–342. https://doi.org/10.1038/sj.leu.2401310
Antipov AA, Sukhorukov GB, Möhwald H (2003) Influence of the ionic strength on the polyelectrolyte multilayers’ permeability. Langmuir 19(6):2444–2448
Apolinário AC, Magoń MS, Pessoa A Jr, Rangel-Yagui CDO (2018) Challenges for the self-assembly of poly (ethylene glycol)–poly (lactic acid)(PEG-PLA) into polymersomes: beyond the theoretical paradigms. Nano 8(6):373
ARENS A, RAUENBUSCH E, IRION E, WAGNER O, BAUER K, KAUFMANN W (1970) Isolation and properties of L-asparaginases from Escherichia coli. Hoppe-Seyler´ s Zeitschrift für Physiologische Chemie 351(1):197–212
Ardalan N, Mirzaie S, Sepahi A, Khavari-Nejad RA (2018) Novel mutant of Escherichia coli asparaginase II to reduction of the glutaminase activity in treatment of acute lymphocytic leukemia by molecular dynamics simulations and QM-MM studies. Medical hypotheses 112:7–17
Arjun JK, Aneesh B, Kavitha T, Hari Krishnan K (2016) Therapeutic L-asparaginase activity of bacteria isolated from marine sediments. Int J Pharmac Sci Drug Res 8(4):229–234
Aslanian AM, Kilberg MS (2001) Multiple adaptive mechanisms affect asparagine synthetase substrate availability in asparaginase-resistant MOLT-4 human leukaemia cells. Biochem J 358(1):59–67
Asselin BL et al (1999) Prognostic significance of early response to a single dose of Asparaginase in childhood acute lymphoblastic. Leukemia 21(1):6–12
Ates B, Ulu A, Köytepe S, Noma SAA, Kolat VS, Izgi T (2018) Magnetic-propelled Fe 3 O 4–chitosan carriers enhance L-asparaginase catalytic activity: a promising strategy for enzyme immobilization. RSC Adv 8(63):36063–36075
Avramis VI, Sencer S, Periclou AP, Sather H, Bostrom BC, Cohen LJ et al (2002) A randomized comparison of nativeEscherichia coli asparaginase and polyethylene glycol conjugated asparaginase for treatment of children with newly diagnosed standard-risk acute lymphoblastic leukemia: a Children’s Cancer Group study. Blood 99(6):1986–1994
Bader RA, Wardwell PR (2014) Polysialic acid: overcoming the hurdles of drug delivery. Ther Deliv 5:235–237. https://doi.org/10.4155/tde.13.153
Badoei-Dalfard A (2015) Purification and characterization of L-asparaginase from Pseudomonas aeruginosa strain SN004: production optimization by statistical methods. Biocatal Agric Biotechnol 4:388–397. https://doi.org/10.1016/j.bcab.2015.06.007
Bahreini E, Aghaiypour K, Abbasalipourkabir R et al (2014) Preparation and nanoencapsulation of L-asparaginase II in chitosan-tripolyphosphate nanoparticles and in vitro release study. Nanoscale Res Lett 9:1–13. https://doi.org/10.1186/1556-276X-9-340
Bai Aswathanarayan J, Rai Vittal R, Muddegowda U (2018) Anticancer activity of metal nanoparticles and their peptide conjugates against human colon adenorectal carcinoma cells. Artif Cells Nanomed Biotechnol 46(7):1444–1451
Balasubramanian MN, Butterworth EA, Kilberg MS (2013) Asparagine synthetase: Regulation by cell stress and involvement in tumor biology. Am J Physiol Endocrinol Metab 304(8):E789–E799. https://doi.org/10.1152/ajpendo.00015.2013
Banerji J (2015) Asparaginase treatment side-effects may be due to genes with homopolymeric Asn codons (Review-Hypothesis). Int J Mol Med 36:607–625. https://doi.org/10.3892/ijmm.2015.2285
Barenholz Y (2001) Liposome application: problems and prospects. Curr Opin Colloid Interface Sci 6(1):66–77
Basha NS, Rekha R, Komala M, Ruby S (2009) Production of extracellular anti-leukaemic enzyme lasparaginase from marine actinomycetes by solidstate and submerged fermentation: purification and characterisation. Trop J Pharm Res 8(4)
Battistel AP, da Rocha BS, dos Santos MT et al (2020) Allergic reactions to asparaginase: retrospective cohort study in pediatric patients with acute lymphoid leukemia. Hematol Transfus Cell Ther 43:9–14. https://doi.org/10.1016/j.htct.2019.10.007
Bergmann S, Lawler SE, Qu Y, Fadzen CM, Wolfe JM, Regan MS et al (2018) Blood–brain-barrier organoids for investigating the permeability of CNS therapeutics. Nat Protoc 13(12):2827–2843
Bhargavi M, Jayamadhuri R (2016) Isolation and screening of marine bacteria producing anti-cancer enzyme L-asparaginase. Am J Mar Sci 4:1–3. https://doi.org/10.12691/marine-4-1-1
Birolli WG, Lima RN, Porto ALM (2019) Applications of marine-derived microorganisms and their enzymes in biocatalysis and biotransformation, the underexplored potentials. Front Microbiol 10:1453. https://doi.org/10.3389/fmicb.2019.01453
Blackman LD, Varlas S, Arno MC, Fayter A, Gibson MI, O’Reilly RK (2017) Permeable protein-loaded polymersome cascade nanoreactors by polymerization-induced self-assembly. ACS Macro Lett 6(11):1263–1267
Blackman LD, Varlas S, Arno MC, Houston ZH, Fletcher NL, Thurecht KJ et al (2018) Confinement of therapeutic enzymes in selectively permeable polymer vesicles by polymerization-induced self-assembly (PISA) reduces antibody binding and proteolytic susceptibility. ACS Central Sci 4(6):718–723
Bonthron DT (1990) L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene. Gene 91:101–105. https://doi.org/10.1016/0378-1119(90)90168-Q
Broome JD (1963) Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects: I. properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance. The Journal of experimental medicine 118(1):99
Broome JD (1965) Antilymphoma activity of L-asparaginase in vivo : clearance rates of enzyme prepara- tions from guinea pig serum and yeast in relation to their effect on tumor growth 1. J Natl Cancer Inst 35:967–974
Bueno CZ, Apolinário AC, Duro-Castano A, Poma A, Pessoa A Jr, Rangel-Yagui CO, Battaglia G (2020) L-asparaginase encapsulation into asymmetric permeable polymersomes. ACS Macro Lett 9:1471–1477
Cammack KA, Marlborough DI, Miller DS (1972) Physical properties and subunit structure of L-asparaginase isolated from Erwinia carotovora. Biochem J 126(2):361–379
Cao Z, Zhang L, Liang K, Cheong S, Boyer C, Gooding JJ et al (2018) Biodegradable 2D Fe–Al hydroxide for nanocatalytic tumor-dynamic therapy with tumor specificity. Adv Sci 5(11):1801155
Chan WK, Lorenzi PL, Anishkin A, Purwaha P, Rogers DM, Sukharev S et al (2014) The glutaminase activity of L-asparaginase is not required for anticancer activity against ASNS-negative cells. Blood 123(23):3596–3606
Chan WK, Horvath TD, Tan L, Link T, Harutyunyan KG, Pontikos MA et al (2019) Glutaminase activity of L-asparaginase contributes to durable preclinical activity against acute lymphoblastic leukemia. Mol Cancer Ther 18(9):1587–1592
Cheng TH, Ismail N, Kamaruding N et al (2020) Industrial enzymes-producing marine bacteria from marine resources. Biotechnol Rep 27:e00482. https://doi.org/10.1016/j.btre.2020.e00482
Chien WW, Le Beux C, Rachinel N et al (2015) Differential mechanisms of asparaginase resistance in B-type acute lymphoblastic leukemia and malignant natural killer cell lines. Sci Rep 5:19–21. https://doi.org/10.1038/srep08068
Choi YJ, Park SJ, Park YS, Park HS, Yang KM, Heo K (2018) EpCAM peptide-primed dendritic cell vaccination confers significant anti-tumor immunity in hepatocellular carcinoma cells. PLoS One 13(1):e0190638
Clementi A (1922) La désamidation enzymatique de l’asparagine chez les différentes espéces animales et la signification physio logique de sa presence dans l’organisme. Arch Int Physiol 19(4):369–398
Cristóvão RO, Almeida MR, Barros MA, Nunes JC, Boaventura RA, Loureiro JM et al (2020) Development and characterization of a novel L-asparaginase/MWCNT nanobioconjugate. RSC Adv 10(52):31205–31213
Darvishi F, Faraji N, Shamsi F (2019) Production and structural modeling of a novel asparaginase in Yarrowia lipolytica. Int J Biol Macromol 125:955–961. https://doi.org/10.1016/j.ijbiomac.2018.12.162
Das S, Lyla PS, Khan SA (2006) Marine microbial diversity and ecology: Importance and future perspectives. Curr Sci 90:1325–1335
Dawidczyk CM, Russell LM, Searson PC (2014) Nanomedicines for cancer therapy: state-of-the-art and limitations to pre-clinical studies that hinder future developments. Front Chem 2:69
Dawidczyk CM, Russell LM, Searson PC (2015) Recommendations for benchmarking preclinical studies of nanomedicines. Cancer Res 75(19):4016–4020
de Almeida Pachioni-Vasconcelos J, Lopes AM, Apolinário AC, Valenzuela-Oses JK, Costa JSR, de Oliveira Nascimento L et al (2016) Nanostructures for protein drug delivery. Biomater Sci 4(2):205–218
de Brito AEM, Pessoa A Jr, Converti A, de Oliveira Rangel-Yagui C, da Silva JA, Apolinário AC (2019) Poly (lactic-co-glycolic acid) nanospheres allow for high L-asparaginase encapsulation yield and activity. Mater Sci Eng C 98:524–534
Dellinger CT, Miale TD (1976) Comparison of anaphylactic reactions to asparaginase derived from Escherichia coli and from Erwinia culturs. Cancer 38(4):1843–1846
Demirgöz D, Pangburn TO, Davis KP, Lee S, Bates FS, Kokkoli E (2009) PR_b-targeted delivery of tumor necrosis factor-α by polymersomes for the treatment of prostate cancer. Soft Matter 5(10):2011–2019
Dhevagi P, Poorani E (2006) Isolation and characterization of L-asparaginase from marine actinomycetes. Indian J Biotechnol 5:514–520
Do TT, Do TP, Nguyen TN et al (2019) Nanoliposomal L-asparaginase and its antitumor activities in lewis lung carcinoma tumor-induced BALB/c mice. Adv Mater Sci Eng 2019. https://doi.org/10.1155/2019/3534807
Dolowy WC, Henson D, Cornet J, Sellin H (1966) Toxic and antineoplastic effects of L-asparaginase: study of mice with lymphoma and normal monkeys and report on a child with leukemia. Cancer 19(12):1813–1819
Dong S, Dong Y, Jia T, Liu S, Liu J, Yang D et al (2020) GSH-depleted nanozymes with hyperthermia-enhanced dual enzyme-mimic activities for tumor nanocatalytic therapy. Adv Mater 32(42):2002439
Dos Santos C, Hamadat S, Le Saux K, Newton C, Mazouni M, Zargarian L et al (2017) Studies of the antitumor mechanism of action of dermaseptin B2, a multifunctional cationic antimicrobial peptide, reveal a partial implication of cell surface glycosaminoglycans. PLoS One 12(8):e0182926
Duval M, Suciu S, Ferster A et al (2002) Comparison of Escherichia coli-asparaginase with Erwinia-asparaginase in the treatment of childhood lymphoid malignancies: results of a randomized European Organisation for Research and Treatment of Cancer - Children’s Leukemia Group phase 3 trial. Blood 99:2734–2739. https://doi.org/10.1182/blood.V99.8.2734
Einsfeldt K, Baptista IC, Pereira JCCV, Costa-Amaral IC, Costa ESD, Ribeiro MCM, ... Almeida RV (2016) Recombinant L-asparaginase from Zymomonas mobilis: a potential new antileukemic agent produced in Escherichia coli. PloS one 11(6):e0156692
Ekladious I, Colson YL, Grinstaff MW (2019) Polymer–drug conjugate therapeutics: advances, insights and prospects. Nat Rev Drug Discov 18:273–294. https://doi.org/10.1038/s41573-018-0005-0
El-Sharkawy AS, Farag AM, Embaby AM et al (2016) Cloning, expression and characterization of aeruginosa EGYII L-Asparaginase from Pseudomonas aeruginosa strain EGYII DSM 101801 in E. coli BL21(DE3) pLysS. J Mol Catal B Enzym 132:16–23. https://doi.org/10.1016/j.molcatb.2016.06.011
Epp O, Steigemann W, Formanek H, Huber R (1971) Crystallographic evidence for the tetrameric subunit structure of L-asparaginase from Escherichia coli. Eur J Biochem 20:432–437
Evans WE (1982) Anaphylacfoid Reactions to Escherichia coli and Erwinia Asparaginase in children with leukemia and lymphoma. Am Cancer Soc 49:1378–1383
Fan K, Xi J, Fan L, Wang P, Zhu C, Tang Y et al (2018) In vivo guiding nitrogen-doped carbon nanozyme for tumor catalytic therapy. Nat Commun 9(1):1–11
Farahat MG, Amr D, Galal A (2020) Molecular cloning, structural modeling and characterization of a novel glutaminase-free L-asparaginase from Cobetia amphilecti AMI6. Int J Biol Macromol 143:685–695. https://doi.org/10.1016/j.ijbiomac.2019.10.258
Farjadian F, Moghoofei M, Mirkiani S, Ghasemi A, Rabiee N, Hadifar S et al (2018) Bacterial components as naturally inspired nano-carriers for drug/gene delivery and immunization: Set the bugs to work? Biotechnol Adv 36(4):968–985
Fu CH, Sakamoto KM (2007) PEG-asparaginase. Expert opinion on pharmacotherapy 8(12):1977–1984
Gao S, Lin H, Zhang H, Yao H, Chen Y, Shi J (2019) Nanocatalytic tumor therapy by biomimetic dual inorganic nanozyme-catalyzed cascade reaction. Adv Sci 6(3):1801733
Gebauer M, Skerra A (2018) Prospects of PASylation® for the design of protein and peptide therapeutics with extended half-life and enhanced action. Bioorg Med Chem 26(10):2882–2887
Ghosh S, Chaganti SR, Prakasham RS (2012) Polyaniline nanofiber as a novel immobilization matrix for the anti-leukemia enzyme L-asparaginase. J Mol Catal B Enzym 74:132–137. https://doi.org/10.1016/j.molcatb.2011.09.009
Gongora-Benitez M, Tulla-Puche J, Albericio F (2014) Multifaceted roles of disulfide bonds. Peptides as therapeutics. Chem Rev 114(2):901–926
Guarecuco R, Williams RT, Baudrier L, La K, Passarelli MC, Ekizoglu N et al (2020) Dietary thiamine influences L-asparaginase sensitivity in a subset of leukemia cells. Sci Adv 6(41):eabc7120
Haley EE, Fischer GA, Welch AD (1961) The requirement for L-asparagine of mouse leukemia cells L5178Y in culture. Cancer Res 21(4):532–536
Hamidi M, Azadi A, Rafiei P (2006) Pharmacokinetic consequences of pegylation. Drug delivery 13(6):399–409
He H, Ye J, Wang Y et al (2014) Cell-penetrating peptides meditated encapsulation of protein therapeutics into intact red blood cells and its application. J Control Release 176:123–132. https://doi.org/10.1016/j.jconrel.2013.12.019
He H, Lu Y, Qi J, Zhu Q, Chen Z, Wu W (2019) Adapting liposomes for oral drug delivery. Acta Pharm Sin B 9(1):36–48
Hermanova I, Zaliova M, Trka J, Starkova J (2012) Low expression of asparagine synthetase in lymphoid blasts precludes its role in sensitivity to L-asparaginase. Exp Hematol 40(8):657–665
Hijiya N, Van Der Sluis IM (2016) Asparaginase-Associated toxicity in children with acute lymphoblastic leukemia. Leuk Lymphoma 57:748–757. https://doi.org/10.3109/10428194.2015.1101098
Hill JM, Roberts J, Loeb E, Khan A, MacLellan A, Hill RW (1967) L-asparaginase therapy for leukemia and other malignant neoplasms: remission in human leukemia. JAMA 202(9):882–888
Hlozkova K, Pecinova A, Alquezar-Artieda N, Pajuelo-Reguera D, Simcikova M, Hovorkova L et al (2020) Metabolic profile of leukemia cells influences treatment efficacy of L-asparaginase. BMC Cancer 20:1–13
Ho PP, Milikin EB, Bobbitt JL, Grinnan EL, Burck PJ, Frank BH et al (1970) Crystalline L-asparaginase from Escherichia coli B I. Purification and chemical characterization. J Biol Chem 245(14):3708–3715
Horowitz B, Madras BK, Meister A, Old LJ, Boyes EA, Stockert E (1968) Asparagine synthetase activity of mouse leukemias. Science 160(3827):533–535. https://doi.org/10.1126/science.160.3827.533
Huang L, Liu Y, Sun Y, Yan Q, Jiang Z (2014) Biochemical characterization of a novel L-Asparaginase with low glutaminase activity from Rhizomucor miehei and its application in food safety and leukemia treatment. Applied and environmental microbiology 80(5):1561–1569
Huang Y, Ren J, Qu X (2019) Nanozymes: classification, catalytic mechanisms, activity regulation, and applications. Chem Rev 119(6):4357–4412
Huo M, Wang L, Wang Y, Chen Y, Shi J (2019) Nanocatalytic tumor therapy by single-atom catalysts. ACS Nano 13(2):2643–2653
Irion ECKART, Voigt WH (1970) Electron microscopy of L-asparaginase from Escherichia coli. Hoppe Seylers Z Physiol Chem 351(9):1154–1156
Izadpanah Qeshmi F, Javadpour S, Malekzadeh K et al (2014) Persian Gulf is a bioresource of potent L-asparaginase producing bacteria: Isolation & molecular differentiating. Int J Environ Res 8:813–818
Izadpanah Qeshmi F, Rahimzadeh M, Javadpour S, Poodat M (2015) Intracellular L-asparaginase from Bacillus sp. PG02: purification, biochemical characterization and evaluation of optimum pH and temperature. Am J Biochem Biotechnol
Izadpanah F, Homaei A, Fernandes P, Javadpour S (2018) Marine microbial L-asparaginase: biochemistry, molecular approaches and applications in tumor therapy and in food industry. Microbiol Res 208:99–112. https://doi.org/10.1016/j.micres.2018.01.011
Jackman JA, Costa VV, Park S, Real ALC, Park JH, Cardozo PL et al (2018) Therapeutic treatment of Zika virus infection using a brain-penetrating antiviral peptide. Nat Mater 17(11):971–977
Jafari B, Pourseif MM, Barar J, Rafi MA, Omidi Y (2019) Peptide-mediated drug delivery across the blood-brain barrier for targeting brain tumors. Expert Opin Drug Deliv 16(6):583–605
Jeong WJ, Bu J, Han Y, Drelich AJ, Nair A, Král P, Hong S (2020) Nanoparticle conjugation stabilizes and multimerizes β-Hairpin peptides to effectively target PD-1/PD-L1 β-sheet-rich interfaces. J Am Chem Soc 142(4):1832–1837
Jiang W, Zhou Y, Yan D (2015) Hyperbranched polymer vesicles: from self-assembly, characterization, mechanisms, and properties to applications. Chem Soc Rev 44(12):3874–3889
Kamala K, Sivaperumal P (2017) Biomedical applications of enzymes from marine actinobacteria. In: Advances in food and nutrition research, vol 80. Academic Press, pp 107–123
Kaneda Y, Tsutsumi Y, Yoshioka Y, Kamada H, Yamamoto Y, Kodaira H et al (2004) The use of PVP as a polymeric carrier to improve the plasma half-life of drugs. Biomaterials 25(16):3259–3266
Keck CM, Müller RH (2013) Nanotoxicological classification system (NCS)–a guide for the risk-benefit assessment of nanoparticulate drug delivery systems. Eur J Pharm Biopharm 84(3):445–448
Kennedy J, Marchesi JR, Dobson ADW (2008) Marine metagenomics: Strategies for the discovery of novel enzymes with biotechnological applications from marine environments. Microb Cell Factories 7:1–8. https://doi.org/10.1186/1475-2859-7-27
Khamessi O, Mabrouk HB, Othman H, ElFessi-Magouri R, De Waard M, Hafedh M et al (2018) RK, the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins. Int J Biol Macromol 120:1777–1788
Khodaverdi E, Tayarani-Najaran Z, Minbashi E, Alibolandi M, Hosseini J, Sepahi S et al (2019) Docetaxel-loaded mixed micelles and polymersomes composed of poly (caprolactone)-poly (ethylene glycol)(PEG-PCL) and poly (lactic acid)-poly (ethylene glycol)(PEG-PLA): preparation and in-vitro characterization. Iran J Pharmac Res 18(1):142
Kidd JG (1953) Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. J Exp Med 98(6):565–582
Killander D, Dohlwitz A, Engstedt L, Franzen S, Gahrton G, Gullbring B et al (1976) Hypersensitive reactions and antibody formation during L-asparaginase treatment of children and adults with acute leukemia. Cancer 37(1):220–228
Kim IW, Lee JH, Kwon YN, Yun EY, Nam SH, Ahn MY et al (2013) Anticancer activity of a synthetic peptide derived from harmoniasin, an antibacterial peptide from the ladybug Harmonia axyridis. Int J Oncol 43(2):622–628
Kiriyama Y, Kubota M, Takimoto T, Kitoh T, Tanizawa A, Akiyama Y, Mikawa H (1989) Biochemical characterization of U937 cells resistant to L-asparaginase: the role of asparagine synthetase. Leukemia 3(4):294–297
Kotzia GA, Lappa K, Labrou NE (2007) Tailoring structure–function properties of L-asparaginase: engineering resistance to trypsin cleavage. Biochem J 404(2):337–343
Kozielski KL, Rui Y, Green JJ (2016) Non-viral nucleic acid containing nanoparticles as cancer therapeutics. Expert Opin Drug Deliv 13(10):1475–1487
Krishna KK, Bhumika V, Thomas M et al (2013) Oceanospirillum nioense sp. nov., a marine bacterium isolated from sediment sample of Palk bay, India. Antonie Van Leeuwenhoek 103:1015–1021. https://doi.org/10.1007/s10482-013-9881-9
Lang S (1904) Uber desamidierung im Tierkorper. Beitr Chem Physiol Pathol 5:321–345
Lauster D, Glanz M, Bardua M, Ludwig K, Hellmund M, Hoffmann U et al (2017) Multivalent peptide–nanoparticle conjugates for influenza-virus inhibition. Angew Chem Int Ed 56(21):5931–5936
Lazarus H, McCoy TA, Farber S et al (1969) Nutritional requirements of human leukemic cells. Asparagine requirements and the effect of L-asparaginase. Exp Cell Res 57:134–138. https://doi.org/10.1016/0014-4827(69)90377-2
Lee SJ, Lee Y, Park GH, Umasuthan N, Heo SJ, De Zoysa M et al (2016) A newly identified glutaminase-free L-asparaginase (L-ASPG86) from the marine bacterium Mesoflavibacter zeaxanthinifaciens. J Microbiol Biotechnol 26(6):1115–1123
Lee JK, Kang SM, Wang X et al (2019) HAP1 loss confers L-asparaginase resistance in ALL by downregulating the calpain-1-Bid-caspase-3/12 pathway. Blood 133:2222–2232. https://doi.org/10.1182/blood-2018-12-890236
Levine DH, Ghoroghchian PP, Freudenberg J, Zhang G, Therien MJ, Greene MI et al (2008) Polymersomes: a new multi-functional tool for cancer diagnosis and therapy. Methods 46(1):25–32
Li S, Byrne B, Welsh J, Palmer AF (2007) Self-assembled poly (butadiene)-b-poly (ethylene oxide) polymersomes as paclitaxel carriers. Biotechnol Prog 23(1):278–285
Lin T, Zhao X, Zhao S, Yu H, Cao W, Chen W et al (2018) O2-generating MnO2 nanoparticles for enhanced photodynamic therapy of bladder cancer by ameliorating hypoxia. Theranostics 8(4):990
Liscano Y, Oñate-Garzón J, Delgado JP (2020) Peptides with dual antimicrobial–anticancer activity: strategies to overcome peptide limitations and rational design of anticancer peptides. Molecules 25(18):4245
Liu X, Wu F, Ji Y, Yin L (2018) Recent advances in anti-cancer protein/peptide delivery. Bioconjug Chem 30(2):305–324
Liu WJ, Wang H, Peng XW, Wang WD, Liu NW, Wang Y, Lu Y (2018) Asparagine synthetase expression is associated with the sensitivity to asparaginase in extranodal natural killer/T-cell lymphoma in vivo and in vitro. Onco Targets Ther 11:6605
Lomelino CL, Andring JT, McKenna R, Kilberg MS (2017) Asparagine synthetase: function, structure, and role in disease. J Biol Chem 292:19952–19958. https://doi.org/10.1074/jbc.R117.819060
Louzao I, van Hest JC (2013) Permeability effects on the efficiency of antioxidant nanoreactors. Biomacromolecules 14(7):2364–2372
Luk BT, Fang RH, Hu CMJ, Copp JA, Thamphiwatana S, Dehaini D et al (2016) Safe and immunocompatible nanocarriers cloaked in RBC membranes for drug delivery to treat solid tumors. Theranostics 6(7):1004
Maddela NR, Chakraborty S, Prasad R (2021) Nanotechnology for advances in medical microbiology. Springer Singapore (ISBN 978-981-15-9915-6). https://www.springer.com/gp/book/9789811599156
Maita T, Matsuda G (1980) The primary structure of L-asparaginase from Escherichia coli. Hoppe-Seyler´ s Zeitschrift für Physiologische Chemie 361(1):105–118
Maita T, Morokuma K, Matsuda G (1974) Amino acid sequence of L-asparaginase from Escherichia coli. J Biochem 76(6):1351–1354
Mashburn LT, Wriston JC (1964) Tumor inhibitory effect of L-asparaginase from Escherichia coli. Arch Biochem Biophys 105:450–452
Matsueda S, Itoh K, Shichijo S (2018) Antitumor activity of antibody against cytotoxic T lymphocyte epitope peptide of lymphocyte-specific protein tyrosine kinase. Cancer Sci 109(3):611–617
Mazloum-Ravasan S, Madadi E, Fathi Z et al (2020) The effect of Yarrowia lipolytica L-asparaginase on apoptosis induction and inhibition of growth in Burkitt’s lymphoma Raji and acute lymphoblastic leukemia MOLT-4 cells. Int J Biol Macromol 146:193–201. https://doi.org/10.1016/j.ijbiomac.2019.12.156
Meena B, Anburajan L, Vinithkumar NV et al (2016) Molecular expression of L-asparaginase gene from Nocardiopsis alba NIOT-VKMA08 in Escherichia coli: a prospective recombinant enzyme for leukaemia chemotherapy. Gene 590:220–226. https://doi.org/10.1016/j.gene.2016.05.003
Meneguetti GP, Santos JHPM, Obreque KMT, Barbosa CMV, Monteiro G, Farsky SHP et al (2019) Novel site-specific PEGylated L-asparaginase. PLoS One 14(2):e0211951
Mikolajczak DJ, Koksch B (2019) Peptide–gold nanoparticle conjugates as artificial carbonic anhydrase mimics. Catalysts 9(11):903
Miller HK, Balis ME (1969) Glutaminase activity of L-asparagine amidohydrolase. Biochem Pharmacol 18(9):2225–2232
Mostafa Y, Alrumman S, Alamri S et al (2019) Enhanced production of glutaminase-free L-asparaginase by marine Bacillus velezensis and cytotoxic activity against breast cancer cell lines. Electron J Biotechnol 42:6–15. https://doi.org/10.1016/j.ejbt.2019.10.001
Nayak S, Porob S, Fernandes A, Meena RM, Ramaiah N (2014) PCR detection of ansA from marine bacteria and its sequence characteristics from Bacillus tequilensis NIOS4. J Basic Microbiol 54(2):162–168
Neuman RE, Mccoy TA (1956) Dual requirement of Walker carcinosarcoma 256 in vitro for asparagine and glutamine. Science (80- ) 124:124–125. https://doi.org/10.1126/science.124.3212.124
Nguyen TH, Nguyen VD (2017) Characterization and applications of marine microbial enzymes in biotechnology and probiotics for animal health. In Advances in food and nutrition research (Vol. 80, pp. 37–74). Academic Press
North ACT, Wade HE, Cammack KA (1969) Physicochemical studies of L-asparaginase from Erwinia carotovora. Nature (London) 224:594–595
Offman MN, Krol M, Patel N, Krishnan S, Liu J, Saha V, Bates PA (2011) Rational engineering of Lasparaginase reveals importance of dual activity for cancer cell toxicity. Blood, The Journal of the American Society of Hematology 117(5):1614–1621
Old LJ, Boyse EA, Campbell HA, Brodey RS, Fidler J, Teller JD (1967) Treatment of lymphosarcoma in the dog with L-asparaginase. Cancer 20(7):1066–1070
Pachioni-Vasconcelos JDA, Apolinário AC, Lopes AM, Pessoa A Jr, Barbosa LRS, Rangel-Yagui CDO (2020) Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes. Soft Mater 19(2):222–230
Pal I, Brahmkhatri VP, Bera S, Bhattacharyya D, Quirishi Y, Bhunia A, Atreya HS (2016) Enhanced stability and activity of an antimicrobial peptide in conjugation with silver nanoparticle. J Colloid Interface Sci 483:385–393
Paliwal R, Babu RJ, Palakurthi S (2014) Nanomedicine scale-up technologies: feasibilities and challenges. AAPS PharmSciTech 15(6):1527–1534
Pan D, Vargas-Morales O, Zern B, Anselmo AC, Gupta V, Zakrewsky M et al (2016) The effect of polymeric nanoparticles on biocompatibility of carrier red blood cells. PLoS One 11(3):e0152074
Panosyan EH, Seibel NL, Martin-Aragon S, Gaynon PS, Avramis IA, Sather H, ... Avramis VI (2004) Asparaginase antibody and asparaginase activity in children with higher-risk acute lymphoblastic leukemia: Children’s Cancer Group Study CCG-1961. Journal of pediatric hematology/oncology 26(4):217–226
Parmentier JH, Maggi M, Tarasco E et al (2015) Glutaminase activity determines cytotoxicity of L-asparaginases on most leukemia cell lines. Leuk Res 39:757–762. https://doi.org/10.1016/j.leukres.2015.04.008
Patel N, Krishnan S, Offman MN, Krol M, Moss CX, Leighton C et al (2009) A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug L-asparaginase. J Clin Invest 119(7):1964–1973
Peng X, Zhou C, Hou X, Liu Y, Wang Z, Peng X et al (2018) Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. Amino Acids 50(2):241–253
Petersen MA, Hillmyer MA, Kokkoli E (2013) Bioresorbable polymersomes for targeted delivery of cisplatin. Bioconjug Chem 24(4):533–543
Peterson RG, Handschumacher RE, Mitchell MS (1971) Immunological responses to L-asparaginase. J Clin Investig 50(5):1080–1090
Phan H, Taresco V, Penelle J, Couturaud B (2020) Polymerisation-induced self-assembly (PISA) as a straightforward formulation strategy for stimuli-responsive drug delivery systems and biomaterials: recent advances. Biomater Sci
Pieters R, Hunger SP, Boos J et al (2011) L-asparaginase treatment in acute lymphoblastic leukemia. Cancer 117:238–249. https://doi.org/10.1002/cncr.25489
Pola M, Rajulapati SB, Potla Durthi C et al (2018) In silico modelling and molecular dynamics simulation studies on L-asparaginase isolated from bacterial endophyte of Ocimum tenuiflorum. Enzym Microb Technol 117:32–40. https://doi.org/10.1016/j.enzmictec.2018.06.005
Pradhan B, Dash SK, Sahoo S (2013) Screening and characterization of extracelluar L-asparaginase producing Bacillus subtilis strain hswx88, isolated from Taptapani hotspring of Odisha, India. Asian Pac J Trop Biomed 3:936–941. https://doi.org/10.1016/S2221-1691(13)60182-3
Prasad R (2016) Advances and applications through fungal nanobiotechnology. Springer, International Publishing Switzerland (ISBN: 978-3-319-42989-2)
Prasad R (2017) Fungal nanotechnology: applications in agriculture, industry, and medicine. Springer Nature Singapore Pte Ltd. (ISBN 978-3-319-68423-9)
Prasad R (2019a) Microbial nanobionics: Basic research and applications. Springer International Publishing (ISBN 978-3-030-16534-5). https://www.springer.com/gp/book/9783030165338
Prasad R (2019b) Microbial nanobionics: state of art. Springer International Publishing (ISBN 978-3-030-16383-9). https://www.springer.com/gp/book/9783030163822
Prasad R, Pandey R, Barman I (2016) Engineering tailored nanoparticles with microbes: quo vadis. WIREs Nanomed Nanobiotechnol 8:316–330. https://doi.org/10.1002/wnan.1363
Prasad R, Jha A, Prasad K (2018) Exploring the realms of nature for nanosynthesis. Springer International Publishing (ISBN 978-3-319-99570-0). https://www.springer.com/978-3-319-99570-0
Prasad R, Siddhardha B, Dyavaiah M (2020) Nanostructures for antimicrobial and antibiofilm applications. Springer International Publishing (ISBN 978-3-030-40336-2). https://www.springer.com/gp/book/9783030403362
Prihanto AA, Wakayama M (2016) Marine microorganism: an underexplored source of L-asparaginase. Adv Food Nutrit Res 79:1–25
Qian X, Zhang J, Gu Z, Chen Y (2019) Nanocatalysts-augmented Fenton chemical reaction for nanocatalytic tumor therapy. Biomaterials 211:1–13
Rahimzadeh M, Poodat M, Javadpour S, Qeshmi FI, Shamsipour F (2016) Purification, characterization and comparison between two new L-asparaginases from Bacillus PG03 and Bacillus PG04. Open Biochem J 10:35
Ramirez-Paz J, Saxena M, Delinois LJ, JoaquÃn-Ovalle FM, Lin S, Chen Z et al (2018) Site-specific PEGylation crosslinking of L-asparaginase subunits to improve its therapeutic efficiency. BioRxiv 317040
Ramsey JD, Flynn NH (2015) Cell-penetrating peptides transport therapeutics into cells. Pharmacol Ther 154:78–86
Ranjitha VR, Muddegowda U, Ravishankar Rai V (2019) Potent activity of bioconjugated peptide and selenium nanoparticles against colorectal adenocarcinoma cells. Drug Dev Ind Pharm 45(9):1496–1505
Rao L, Tian R, Chen X (2020) Cell-membrane-mimicking nanodecoys against infectious diseases. ACS Nano 14(3):2569–2574
Ravuri J, Kumari K (2013) In vitro anticancer activity of marine bacteria isolated from Andhra Pradesh and Tamil Nadu coastal regions. Int J Chem Environ Biol Sci 1:3–5
Richards NG, Kilberg MS (2006) Asparagine synthetase chemotherapy. Annu Rev Biochem 75:629–654. https://doi.org/10.1146/annurev.biochem.75.103004.142520. PMID: 16756505; PMCID: PMC3587692
Rideau E, Dimova R, Schwille P, Wurm FR, Landfester K (2018) Liposomes and polymersomes: a comparative review towards cell mimicking. Chem Soc Rev 47(23):8572–8610
Roberts J, Prager MD, Bachynsky N (1966) The antitumor activity of Escherichia coli L-asparaginase. Cancer Res 26(10):2213–2217
Rossi L, Pierigè F, Bregalda A, Magnani M (2020) Preclinical developments of enzyme-loaded red blood cells. Expert Opin Drug Deliv
Sabu C, Rejo C, Kotta S, Pramod K (2018) Bioinspired and biomimetic systems for advanced drug and gene delivery. J Control Release 287:142–155
Saeed H, Ali H, Soudan H, Embaby A, El-Sharkawy A, Farag A, ... Ataya F (2018) Molecular cloning, structural modeling and production of recombinant Aspergillus terreus L. asparaginase in Escherichia coli. International journal of biological macromolecules 106:1041–1051
Saeed H, Hemida A, El-Nikhely N et al (2020) Highly efficient Pyrococcus furiosus recombinant L-asparaginase with no glutaminase activity: Expression, purification, functional characterization, and cytotoxicity on THP-1, A549 and Caco-2 cell lines. Int J Biol Macromol 156:812–828. https://doi.org/10.1016/j.ijbiomac.2020.04.080
Saglam N, Korkusuz, F, Prasad R (2021) Nanotechnology applications in health and environmental sciences. Springer International Publishing (ISBN: 978-3-030-64410-9). https://www.springer.com/gp/book/9783030644093
Sarma H, Joshi S, Prasad R, Jampilek J (2021) Biobased nanotechnology for green applications. Springer International Publishing (ISBN 978-3-030-61985-5). https://www.springer.com/gp/book/9783030619848
Schwarzer TS, Klermund L, Wang G, Castiglione K (2018) Membrane functionalization of polymersomes: alleviating mass transport limitations by integrating multiple selective membrane transporters for the diffusion of chemically diverse molecules. Nanotechnology 29(44):44LT01
Shaik M, Sankar GG, Iswarya M, Rajitha P (2017) Isolation and characterization of bioactive metabolites producing marine Streptomyces parvulus strain sankarensis-A10. J Gen Eng Biotechnol 15(1):87–94
Shakambari G, Birendranarayan AK, Angelaa Lincy MJ et al (2016) Hemocompatible glutaminase free L-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression. RSC Adv 6:25943–25951. https://doi.org/10.1039/c6ra00727a
Shi R, Liu Y, Mu Q, Jiang Z, Yang S (2017) Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes. Int J Biol Macromol 96:93–99
Shrivastava A, Khan AA, Khurshid M et al (2016) Recent developments in L-asparaginase discovery and its potential as anticancer agent. Crit Rev Oncol Hematol 100:1–10. https://doi.org/10.1016/j.critrevonc.2015.01.002
Singh M, Hassan N, Verma D, Thakur P, Panda BP, Panda AK et al (2020) Design of expert guided investigation of native L-asparaginase encapsulated long-acting cross-linker-free poly (lactic-co-glycolic) acid nanoformulation in an Ehrlich ascites tumor model. Saudi Pharmac J 28(6):719–728
Soares AL, Guimaraes GM, Polakiewicz B, de Moraes Pitombo RN, Abrahão-Neto J (2002) Effects of polyethylene glycol attachment on physicochemical and biological stability of E. coli L-asparaginase. Int J Pharm 237(1–2):163–170
Srivastava S, Usmani Z, Atanasov AG, Singh VK, Singh NP, Abdel-Azeem AM, Prasad R, Gupta G, Sharma M, Bhargava A (2021) Biological nanofactories: Using living forms for metal nanoparticle synthesis. Mini- Reviews in Medicinal Chemistry 21(2): 245–265
Stams WA, den Boer ML, Beverloo HB, Meijerink JP, Stigter RL, van Wering ER et al (2003) Sensitivity to L-asparaginase is not associated with expression levels of asparagine synthetase in t (12; 21)+ pediatric ALL. Blood J Am Soc Hematol 101(7):2743–2747
Stecher AL, De Deus PM, Polikarpov I, Abrahao-Neto J (1999) Stability of L-asparaginase: an enzyme used in leukemia treatment. Pharm Acta Helv 74(1):1–9
Su N, Pan YX, Zhou M, Harvey RC, Hunger SP, Kilberg MS (2008) Correlation between asparaginase sensitivity and asparagine synthetase protein content, but not mRNA, in acute lymphoblastic leukemia cell lines. Pediatric blood & cancer 50(2):274–279
Sun J, Nagel R, Zaal EA, Ugalde AP, Han R, Proost N, ... Agami R (2019) SLC 1A3 contributes to Lasparaginase resistance in solid tumors. The EMBO journal 38(21):e102147
Sundaramoorthi C, Rajakumari R, Dharamsi ABHAY, Vengadeshprabhu K (2012) Production and immobilization of L-asparaginase from marine source. Int J Pharm Pharm Sci 4:229–232
Sutrisno L, Hu Y, Hou Y, Cai K, Li M, Luo Z (2020) Progress of iron-based nanozymes for antitumor therapy. Front Chem 8
Swain AL, Jaskolski M, Housset D et al (1993) Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc Natl Acad Sci U S A 90:1474–1478. https://doi.org/10.1073/pnas.90.4.1474
Taleghani AS, Ebrahimnejad P, Heidarinasab A, Akbarzadeh A (2019) Sugar-conjugated dendritic mesoporous silica nanoparticles as pH-responsive nanocarriers for tumor targeting and controlled release of deferasirox. Mater Sci Eng C 98:358–368
Tanner P, Onaca O, Balasubramanian V, Meier W, Palivan CG (2011) Enzymatic cascade reactions inside polymeric nanocontainers: a means to combat oxidative stress. Chem Eur J 17(16):4552–4560
Thi TTH, Pilkington EH, Nguyen DH et al (2020) The importance of Poly(ethylene glycol) alternatives for overcoming PEG immunogenicity in drug delivery and bioconjugation. Polymers (Basel) 12(2):298. https://doi.org/10.3390/polym12020298
Tong WH, van der Sluis IM, Alleman CJM et al (2013) Cost-analysis of treatment of childhood acute lymphoblastic leukemia with asparaginase preparations: The impact of expensive chemotherapy. Haematologica 98:753–759. https://doi.org/10.3324/haematol.2012.073510
Tsuchiya N, Hosono A, Yoshikawa T, Shoda K, Nosaka K, Shimomura M et al (2018) Phase I study of glypican-3-derived peptide vaccine therapy for patients with refractory pediatric solid tumors. Onco Targets Ther 7(1):e1377872
Ueno T, Ohtawa K, Mitsui K et al (1997) Cell cycle arrest and apoptosis of leukemia cells induced by L-asparaginase. Leukemia 11:1858–1861. https://doi.org/10.1038/sj.leu.2400834
Ulu A, Ates B (2017) Immobilization of l -asparaginase on carrier materials: a comprehensive review. Bioconjug Chem 28:1598–1610. https://doi.org/10.1021/acs.bioconjchem.7b00217
Ulu A, Koytepe S, Ates B (2016) Design of starch functionalized biodegradable P (MAA-co-MMA) as carrier matrix for l-asparaginase immobilization. Carbohydrate polymers 153:559–572
Ulu A, Noma SAA, Koytepe S, Ates B (2018) Magnetic Fe3O4@ MCM-41 core–shell nanoparticles functionalized with thiol silane for efficient L-asparaginase immobilization. Artif Cells Nanomed Biotechnol 46(sup2):1035–1045
Upadhyay KK, Mishra AK, Chuttani K, Kaul A, Schatz C, Le Meins JF et al (2012) The in vivo behavior and antitumor activity of doxorubicin-loaded poly (γ-benzyl l-glutamate)-block-hyaluronan polymersomes in Ehrlich ascites tumor-bearing BalB/c mice. Nanomedicine 8(1):71–80
Vala AK, Sachaniya B, Dudhagara D et al (2018) International Journal of Biological Macromolecules Characterization of L-asparaginase from marine-derived Aspergillus niger AKV-MKBU, its antiproliferative activity and bench scale production using industrial waste. Int J Biol Macromol 108:41–46. https://doi.org/10.1016/j.ijbiomac.2017.11.114
van Oppen LM, Abdelmohsen LK, van Emst-de Vries SE, Welzen PL, Wilson DA, Smeitink JA et al (2018) Biodegradable synthetic organelles demonstrate ROS shielding in human-complex-I-deficient fibroblasts. ACS Central Sci 4(7):917–928
Varlas S, Blackman LD, Findlay HE, Reading E, Booth PJ, Gibson MI, O’Reilly RK (2018) Photoinitiated polymerization-induced self-assembly in the presence of surfactants enables membrane protein incorporation into vesicles. Macromolecules 51(16):6190–6201
Varlas S, Foster JC, Georgiou PG, Keogh R, Husband JT, Williams DS, O’Reilly RK (2019) Tuning the membrane permeability of polymersome nanoreactors developed by aqueous emulsion polymerization-induced self-assembly. Nanoscale 11(26):12643–12654
Vasile C (2019) Polymeric nanomaterials: recent developments, properties and medical applications. Polymeric nanomaterials in nanotherapeutics, 1-66. Micro and Nano Technologies 235–259
Vimal A, Kumar A (2017) Biotechnological production and practical application of L-asparaginase enzyme. Biotechnol Genet Eng Rev 33:40–61. https://doi.org/10.1080/02648725.2017.1357294
Vina I, Karsakevich A, Bekers M (2001) Stabilization of anti-leukemic enzyme L-asparaginase by immobilization on polysaccharide levan. J Mol Catal B Enzym 11:551–558. https://doi.org/10.1016/S1381-1177(00)00043-6
Wade HE, Elsworth R, Herbert D, Keppie J, Sargeant K (1968) A new L-asparaginase with antitumour activity. Lancet 292(7571):776–777
Wahab RA, Elias N, Abdullah F, Ghoshal SK (2020) On the taught new tricks of enzymes immobilization: An all-inclusive overview. React Funct Polym 152:104613. https://doi.org/10.1016/j.reactfunctpolym.2020.104613
Wang F, Zhang YQ (2015) Bioconjugation of silk fibroin nanoparticles with enzyme and peptide and their characterization. Advances in protein chemistry and structural biology 98:263–291
Wannasarit S, Wang S, Figueiredo P, Trujillo C, Eburnea F, Simón-Gracia L et al (2019) A virus-mimicking pH-responsive acetalated dextran-based membrane-active polymeric nanoparticle for intracellular delivery of antitumor therapeutics. Adv Funct Mater 29(51):1905352
Warrell RP Jr, Arlin ZA, Gee TS, Chou TC, Roberts J, Young CW (1982) Clinical evaluation of succinylated Acinetobacter glutaminase-asparaginase in adult leukemia. Cancer Treat Rep 66(7):1479–1485
Wicki A, Ritschard R, Loesch U, Deuster S, Rochlitz C, Mamot C (2015) Large-scale manufacturing of GMP-compliant anti-EGFR targeted nanocarriers: Production of doxorubicin-loaded anti-EGFR-immunoliposomes for a first-in-man clinical trial. Int J Pharm 484(1–2):8–15
Wilder LM, Handali PR, Webb LJ, Crooks RM (2020) Interactions between oligoethylene glycol-capped AuNPs and attached peptides control peptide structure. Bioconjug Chem
Willems L, Jacque N, Jacquel A, Neveux N, Trovati Maciel T, Lambert M, ... Bouscary D (2013) Inhibiting glutamine uptake represents an attractive new strategy for treating acute myeloid leukemia. Blood, The Journal of the American Society of Hematology 122(20):3521–3532
Williams RT, Guarecuco R, Gates LA, Barrows D, Passarelli MC, Carey B et al (2020) ZBTB1 regulates asparagine synthesis and leukemia cell response to L-asparaginase. Cell Metab 31(4):852–861
Xie X, Zhou W, Hu Y, Chen Y, Zhang H, Li Y (2018) A dual-function epidermal growth factor receptor pathway substrate 8 (Eps8)-derived peptide exhibits a potent cytotoxic T lymphocyte-activating effect and a specific inhibitory activity. Cell Death Dis 9(3):1–16
Xu H, Chen CX, Hu J, Zhou P, Zeng P, Cao CH, Lu JR (2013) Dual modes of antitumor action of an amphiphilic peptide A(9)K. Biomaterials 34(11):2731–2737. https://doi.org/10.1016/j.biomaterials.2012.12.039. Epub 2013 Jan 23
Xu B, Cui Y, Wang W, Li S, Lyu C, Wang S et al (2020) Immunomodulation-enhanced nanozyme-based tumor catalytic therapy. Adv Mater 32(33):2003563
Zhang YQ, Tao ML, De Shen W et al (2004) Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters. Biomaterials 25:3751–3759. https://doi.org/10.1016/j.biomaterials.2003.10.019
Zhang B, Shi W, Li J, Liao C, Yang L, Huang W, Qian H (2017) Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities. Chem Biol Drug Des 90(5):972–980
Zhang K, Tang X, Zhang J, Lu W, Lin X, Zhang Y, ... He H (2014) PEG–PLGA copolymers: Their structure and structure-influenced drug delivery applications. Journal of Controlled release 183:77–86
Zhao Y, Ding B, Xiao X, Jiang F, Wang M, Hou Z et al (2020) Virus-like Fe3O4@ Bi2S3 nanozymes with resistance-free apoptotic hyperthermia-augmented nanozymitic activity for enhanced synergetic cancer therapy. ACS Appl Mater Interfaces 12(10):11320–11328
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Switzerland AG
About this chapter
Cite this chapter
Chakravarty, N., Mathur, A., Singh, R.P. (2022). L-asparaginase: Insights into the Marine Sources and Nanotechnological Advancements in Improving Its Therapeutics. In: Sarma, H., Gupta, S., Narayan, M., Prasad, R., Krishnan, A. (eds) Engineered Nanomaterials for Innovative Therapies and Biomedicine. Nanotechnology in the Life Sciences. Springer, Cham. https://doi.org/10.1007/978-3-030-82918-6_4
Download citation
DOI: https://doi.org/10.1007/978-3-030-82918-6_4
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-82917-9
Online ISBN: 978-3-030-82918-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)