3/28/2023 0 Comments Farsky beta size![]() Received: AugAccepted: JanuPublished: February 12, 2019Ĭopyright: © 2019 Meneguetti et al. PLoS ONE 14(2):Įditor: Marco Rito-Palomares, Tecnologico de Monterrey, MEXICO (2019) Novel site-specific PEGylated L-asparaginase. monoPEG-ASNase demonstrates its potential as a novel option for ALL treatment, being an inventive novelty that maintains the benefits of the current enzyme and solves challenges.Ĭitation: Meneguetti GP, Santos JHPM, Obreque KMT, Barbosa CMV, Monteiro G, Farsky SHP, et al. Additionally, monoPEG-ASNase was found to be potent against leukemic cell lines (MOLT-4 and REH) in vitro like polyPEG-ASNase. The monoPEG-ASNase was found to maintain enzymatic stability for more days than ASNase, also was resistant to the plasma proteases like asparaginyl endopeptidase and cathepsin B. The highest yield of monoPEG-ASNase of 42% was obtained by the protein reaction with methoxy polyethylene glycol-carboxymethyl N-hydroxysuccinimidyl ester (10kDa) in 100 mM PBS at pH 7.5 and PEG:ASNase ratio of 25:1. ![]() The monoPEG-ASNase was purified by anionic followed by size exclusion chromatography to a final purity of 99%. In this work we developed a site-specific N-terminus PEGylation protocol for ASNase. However, pegaspargase is randomly PEGylated and, consequently, with a high degree of polydispersity in its final formulation. PEGylation refers to the covalent attachment of poly(ethylene) glycol to the protein drug and it not only reduces the immune system activation but also decreases degradation by plasmatic proteases. L-asparaginase (ASNase) from Escherichia coli is currently used in some countries in its PEGylated form (ONCASPAR, pegaspargase) to treat acute lymphoblastic leukemia (ALL).
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