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Cysteine-Selective Modification of Peptides and Proteins via Desulfurative C-C Bond Formation.


ABSTRACT: The site-selective modification of peptides and proteins facilitates the preparation of targeted therapeutic agents and tools to interrogate biochemical pathways. Among the numerous bioconjugation techniques developed to install groups of interest, those that generate C(sp3 )-C(sp3 ) bonds are significantly underrepresented despite affording proteolytically stable, biogenic linkages. Herein, a visible-light-mediated reaction is described that enables the site-selective modification of peptides and proteins via desulfurative C(sp3 )-C(sp3 ) bond formation. The reaction is rapid and high yielding in peptide systems, with comparable translation to proteins. Using this chemistry, a range of moieties is installed into model systems and an effective PTM-mimic is successfully integrated into a recombinantly expressed histone.

SUBMITTER: Griffiths RC 

PROVIDER: S-EPMC10946470 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature

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Cysteine-Selective Modification of Peptides and Proteins via Desulfurative C-C Bond Formation.

Griffiths Rhys C RC   Smith Frances R FR   Li Diyuan D   Wyatt Jasmine J   Rogers David M DM   Long Jed E JE   Cusin Lola M L LML   Tighe Patrick J PJ   Layfield Robert R   Hirst Jonathan D JD   Müller Manuel M MM   Mitchell Nicholas J NJ  

Chemistry (Weinheim an der Bergstrasse, Germany) 20230214 16


The site-selective modification of peptides and proteins facilitates the preparation of targeted therapeutic agents and tools to interrogate biochemical pathways. Among the numerous bioconjugation techniques developed to install groups of interest, those that generate C(sp<sup>3</sup> )-C(sp<sup>3</sup> ) bonds are significantly underrepresented despite affording proteolytically stable, biogenic linkages. Herein, a visible-light-mediated reaction is described that enables the site-selective modi  ...[more]

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