A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification

Local protein microenvironment is used to control the outcome of reaction between cysteine residues and 2,5-dibromohexanediamide. The differential reactivity is exploited to introduce two orthogonal reactive handles onto the surface of a double cysteine mutant of superfolder green fluorescent protei...

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Detalles Bibliográficos
Autores principales: Nathani, Ramiz I., Moody, Paul, Chudasama, Vijay, Smith, Mark E. B., Fitzmaurice, Richard J., Caddick, Stephen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2013
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985185/
https://www.ncbi.nlm.nih.gov/pubmed/24741436
http://dx.doi.org/10.1039/c3sc51333e
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author Nathani, Ramiz I.
Moody, Paul
Chudasama, Vijay
Smith, Mark E. B.
Fitzmaurice, Richard J.
Caddick, Stephen
author_facet Nathani, Ramiz I.
Moody, Paul
Chudasama, Vijay
Smith, Mark E. B.
Fitzmaurice, Richard J.
Caddick, Stephen
author_sort Nathani, Ramiz I.
collection PubMed
description Local protein microenvironment is used to control the outcome of reaction between cysteine residues and 2,5-dibromohexanediamide. The differential reactivity is exploited to introduce two orthogonal reactive handles onto the surface of a double cysteine mutant of superfolder green fluorescent protein in a regioselective manner. Subsequent elaboration with commonly used thiol and alkyne containing reagents affects site-selective protein dual labelling.
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spelling pubmed-39851852014-04-14 A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification Nathani, Ramiz I. Moody, Paul Chudasama, Vijay Smith, Mark E. B. Fitzmaurice, Richard J. Caddick, Stephen Chem Sci Chemistry Local protein microenvironment is used to control the outcome of reaction between cysteine residues and 2,5-dibromohexanediamide. The differential reactivity is exploited to introduce two orthogonal reactive handles onto the surface of a double cysteine mutant of superfolder green fluorescent protein in a regioselective manner. Subsequent elaboration with commonly used thiol and alkyne containing reagents affects site-selective protein dual labelling. Royal Society of Chemistry 2013-07-29 2013-06-18 /pmc/articles/PMC3985185/ /pubmed/24741436 http://dx.doi.org/10.1039/c3sc51333e Text en This journal is © The Royal Society of Chemistry 2013 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
Nathani, Ramiz I.
Moody, Paul
Chudasama, Vijay
Smith, Mark E. B.
Fitzmaurice, Richard J.
Caddick, Stephen
A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title_full A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title_fullStr A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title_full_unstemmed A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title_short A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
title_sort novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985185/
https://www.ncbi.nlm.nih.gov/pubmed/24741436
http://dx.doi.org/10.1039/c3sc51333e
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