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Issue 19, 2011
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Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis

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Abstract

Controlling maleimide hydrolysis allows the modular construction of bromomaleimide-mediated bioconjugates which are either stable or cleavable in an aqueous, thiol-mediated reducing environment. The application of this methodology to reversible protein biotinylation, the irreversible labeling of peptide disulfide bonds and the assembly of stable, fluorescein-labelled glycoprotein mimics is described.

Graphical abstract: Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis

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Supplementary files

Article information


Submitted
24 Feb 2011
Accepted
22 Mar 2011
First published
05 Apr 2011

This article is Open Access

Chem. Commun., 2011,47, 5452-5454
Article type
Communication

Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis

C. P. Ryan, M. E. B. Smith, F. F. Schumacher, D. Grohmann, D. Papaioannou, G. Waksman, F. Werner, J. R. Baker and S. Caddick, Chem. Commun., 2011, 47, 5452
DOI: 10.1039/C1CC11114K

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