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Bromopyridazinedione-mediated protein and peptide bioconjugation
Bromopyridazinedione-mediated bioconjugation to a cysteine containing protein and a disulfide containing peptide is described. The conjugates are cleavable in an excess of thiol, including cytoplasmically-relevant concentrations of glutathione, and show a high level of hydrolytic stability. The cons...
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/PMC3379626/ https://www.ncbi.nlm.nih.gov/pubmed/21738916 http://dx.doi.org/10.1039/c1cc12807h |
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author | Chudasama, Vijay Smith, Mark E. B. Schumacher, Felix F. Papaioannou, Danai Waksman, Gabriel Baker, James R. Caddick, Stephen |
author_facet | Chudasama, Vijay Smith, Mark E. B. Schumacher, Felix F. Papaioannou, Danai Waksman, Gabriel Baker, James R. Caddick, Stephen |
author_sort | Chudasama, Vijay |
collection | PubMed |
description | Bromopyridazinedione-mediated bioconjugation to a cysteine containing protein and a disulfide containing peptide is described. The conjugates are cleavable in an excess of thiol, including cytoplasmically-relevant concentrations of glutathione, and show a high level of hydrolytic stability. The constructs have the potential for four points of chemical attachment. |
format | Online Article Text |
id | pubmed-3379626 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-33796262012-06-20 Bromopyridazinedione-mediated protein and peptide bioconjugation Chudasama, Vijay Smith, Mark E. B. Schumacher, Felix F. Papaioannou, Danai Waksman, Gabriel Baker, James R. Caddick, Stephen Chem Commun (Camb) Chemistry Bromopyridazinedione-mediated bioconjugation to a cysteine containing protein and a disulfide containing peptide is described. The conjugates are cleavable in an excess of thiol, including cytoplasmically-relevant concentrations of glutathione, and show a high level of hydrolytic stability. The constructs have the potential for four points of chemical attachment. Royal Society of Chemistry 2011-08-21 2011-07-07 /pmc/articles/PMC3379626/ /pubmed/21738916 http://dx.doi.org/10.1039/c1cc12807h 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 Chudasama, Vijay Smith, Mark E. B. Schumacher, Felix F. Papaioannou, Danai Waksman, Gabriel Baker, James R. Caddick, Stephen Bromopyridazinedione-mediated protein and peptide bioconjugation |
title | Bromopyridazinedione-mediated protein and peptide bioconjugation
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title_full | Bromopyridazinedione-mediated protein and peptide bioconjugation
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title_fullStr | Bromopyridazinedione-mediated protein and peptide bioconjugation
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title_full_unstemmed | Bromopyridazinedione-mediated protein and peptide bioconjugation
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title_short | Bromopyridazinedione-mediated protein and peptide bioconjugation
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title_sort | bromopyridazinedione-mediated protein and peptide bioconjugation |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3379626/ https://www.ncbi.nlm.nih.gov/pubmed/21738916 http://dx.doi.org/10.1039/c1cc12807h |
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