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Article

Cysteine Pegylation of a Mutant L-asparaginase Affords Enhanced Activity and Thermostability. A Comparative Study Against N-terminal Conjugation.

Applied biochemistry and biotechnology - 1 Apr 2026

Ferraro Rafael B, Benevides Guilherme R, Rabelo Jheniffer, da Silva Chaves Flaviana, Ruiz-Lara Grace Veronica, Carretero Gustavo, Monteiro Gisele, Pessoa-Junior Adalberto, Converti Attilio, Lynham Steven, Long Paul F, Rangel-Yagui Carlota O

Abstract excerpt

L-asparaginase (ASNase) is one of the most clinically relevant biopharmaceuticals but proteolysis impairs the enzyme half-life. ASNase P40S/S206C was developed to overcome proteolysis and in addition pegylation can be used to improve half-life and thermostability. Here Cys206 and N-terminal residues were explored as pegylation sites for a potential new biobetter. Optimal mono-pegylation of Cys (Cys-PEG-ASNase)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41653260
DOI: 10.1007/s12010-025-05545-1
PMCID: PMC13032998

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