Evidence map›Paper›PMID 41653260›Full record

ArticleApplied biochemistry and biotechnology2026

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

Rafael B Ferraro, Guilherme R Benevides, Jheniffer Rabelo, Flaviana da Silva Chaves, Grace Veronica Ruiz-Lara, Gustavo Carretero, Gisele Monteiro, Adalberto Pessoa-Junior, Attilio Converti, Steven Lynham and 2 more

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Rafael B FerraroDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Guilherme R BenevidesDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Jheniffer RabeloDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Flaviana da Silva ChavesDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Grace Veronica Ruiz-LaraDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Gustavo CarreteroInstitute of Chemistry, University of São Paulo, São Paulo, Brazil.
Gisele MonteiroDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Adalberto Pessoa-JuniorDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil.
Attilio ConvertiUniversity of Genoa, Genoa, Italy.
Steven LynhamProteomics Core Facility, The James Black Center, King's College London, London, UK.
Paul F LongInstitute of Pharmaceutical Science, Faculty of Life Sciences & Medicine, King's College London, London, UK.
Carlota O Rangel-YaguiDepartment of Biochemical Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo, Brazil. corangel@usp.br.ORCID http://orcid.org/0000-0003-4221-9505

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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) provided similar yields compared to N-terminal mono-pegylation (NT-PEG-ASNase) but at lower PEG concentration. Specific activity was higher for Cys-PEG-ASNase than NT-PEG-ASNase. The role of pegylation site in activity was confirmed by activation energy (Ea) and enthalpy variation (ΔH

Indexed as

AsparaginaseCysteineMutationPolyethylene GlycolsTemperatureEnzyme StabilityThermodynamicsAsparaginaseCysteinePolyethylene GlycolsEnzymatic activityEnzyme stabilityL-AsparaginasePegylationThermodynamicsThermostability

Identifiers

PMID41653260
PMCPMC13032998

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.