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

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 pep...

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Autores principales: Ryan, Chris P., Smith, Mark E. B., Schumacher, Felix F., Grohmann, Dina, Papaioannou, Danai, Waksman, Gabriel, Werner, Finn, Baker, James R., Caddick, Stephen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3381635/
https://www.ncbi.nlm.nih.gov/pubmed/21465057
http://dx.doi.org/10.1039/c1cc11114k
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author Ryan, Chris P.
Smith, Mark E. B.
Schumacher, Felix F.
Grohmann, Dina
Papaioannou, Danai
Waksman, Gabriel
Werner, Finn
Baker, James R.
Caddick, Stephen
author_facet Ryan, Chris P.
Smith, Mark E. B.
Schumacher, Felix F.
Grohmann, Dina
Papaioannou, Danai
Waksman, Gabriel
Werner, Finn
Baker, James R.
Caddick, Stephen
author_sort Ryan, Chris P.
collection PubMed
description 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.
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spelling pubmed-33816352012-06-25 Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis Ryan, Chris P. Smith, Mark E. B. Schumacher, Felix F. Grohmann, Dina Papaioannou, Danai Waksman, Gabriel Werner, Finn Baker, James R. Caddick, Stephen Chem Commun (Camb) Chemistry 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. Royal Society of Chemistry 2011-05-21 2011-04-05 /pmc/articles/PMC3381635/ /pubmed/21465057 http://dx.doi.org/10.1039/c1cc11114k Text en This journal is © The Royal Society of Chemistry 2011 http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Ryan, Chris P.
Smith, Mark E. B.
Schumacher, Felix F.
Grohmann, Dina
Papaioannou, Danai
Waksman, Gabriel
Werner, Finn
Baker, James R.
Caddick, Stephen
Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title_full Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title_fullStr Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title_full_unstemmed Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title_short Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
title_sort tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3381635/
https://www.ncbi.nlm.nih.gov/pubmed/21465057
http://dx.doi.org/10.1039/c1cc11114k
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