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Updated: Jan 11, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
Published on: July 20, 2016
Chemoselective Methionine Bioconjugation with Hydroxylamine Esters for Peptide/Protein Modifications
Man Li1,2, Tianyang Wang2, Linfeng Chen2
1School of Pharmacy, Hubei University of Science and Technology, Xianning 437100, China.
Researchers developed a green bioconjugation method using a new reagent that selectively modifies methionine in proteins and peptides. This simple approach offers a robust tool for peptide and protein modification under aqueous conditions.
Area of Science:
- Biochemistry
- Organic Chemistry
- Chemical Biology
Background:
- Bioconjugation is essential for modifying proteins and peptides.
- Methionine's thioether group is a key site for bioconjugation due to its nucleophilicity.
Purpose of the Study:
- To develop a novel, simple, and green bioconjugation reagent.
- To achieve methionine-selective modification of peptides and proteins under aqueous conditions.
Main Methods:
- Synthesis of a new hydroxylamine ester reagent.
- Application of the reagent for bioconjugation under aqueous conditions.
- Utilizing a carboxylic acid group for tunable stabilization of the aza-sulfonium adduct.
Main Results:
- A simple and green bioconjugation reagent was successfully developed.
- The reagent demonstrates high selectivity for methionine residues.
- The method is robust and effective under aqueous conditions.
Conclusions:
- The new hydroxylamine ester provides a valuable and simple tool for methionine-selective bioconjugation.
- This method facilitates peptide and protein modification with enhanced stability.
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