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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2011
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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. |
format | Online Article Text |
id | pubmed-3381635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
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
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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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