Site‐Selective Installation of N ϵ ‐Modified Sidechains into Peptide and Protein Scaffolds via Visible‐Light‐Mediated Desulfurative C–C Bond Formation

Autor:	Jed Long, Frances R. Smith, Nick Mitchell, Huw E. L. Williams, Daniel Scott, Rhys C. Griffiths, Robert Layfield, Neil J. Oldham
Rok vydání:	2021
Předmět:	chemistry.chemical_classification Peptide modification Protein function Bioconjugation biology Chemistry Stereochemistry Lysine Peptide General Chemistry General Medicine Bond formation Catalysis Ubiquitin biology.protein Cysteine
Zdroj:	Angewandte Chemie. 134
ISSN:	1521-3757 0044-8249
DOI:	10.1002/ange.202110223
Popis:	Post-translational modifications (PTMs) enhance the repertoire of protein function and mediate or influence the activity of the majority of cellular processes. The preparation of site-specifically and homogeneously modified proteins to apply as tools to understand the biological role of PTMs is a challenging task. Herein, we describe a visible-light-mediated desulfurative C(sp3)-C(sp3) bond forming reaction that enables the site-selective installation of Ne-modified sidechains into peptides and proteins of interest. Rapid, operationally simple and tolerant to ambient atmosphere, we demonstrate the installation of a range of lysine (Lys) PTMs into model peptide systems and showcase the potential of this technology by site- selectively installing an NeAc sidechain into recombinantly expressed ubiquitin (Ub).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28aebb0286bbfaf5de09f57d7f5e7297 https://doi.org/10.1002/ange.202110223 Zobrazit plný text záznamu