Issue 19, 2011
From the journal:

Chemical Communications

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

Chris P. Ryan,a   Mark E. B. Smith,a   Felix F. Schumacher,a   Dina Grohmann,b   Danai Papaioannou,c   Gabriel Waksman,c   Finn Werner,b   James R. Baker*a  and  Stephen Caddick*a  

* Corresponding authors

a Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK
E-mail: s.caddick@ucl.ac.uk
Tel: +44 (0)20 3108 5071

b Research Department of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK

c Institute of Structural and Molecular Biology at UCL/Birkbeck, Malet Street, London WC1E 7HX, UK

Abstract

Controlling maleimidehydrolysis 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 proteinbiotinylation, the irreversible labeling of peptidedisulfide 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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Article information

DOI
https://doi.org/10.1039/C1CC11114K
Article type
Communication
Submitted
24 Feb 2011
Accepted
22 Mar 2011
First published
05 Apr 2011
This article is Open Access

Chem. Commun., 2011,47, 5452-5454

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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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