Open AccessLight‐Driven Diselenide Metathesis in Peptides
Author(s) -
Waliczek Mateusz,
Pehlivan Özge,
Stefanowicz Piotr
Publication year - 2019
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.201900224
Subject(s) - diselenide , metathesis , selenocysteine , chemistry , cysteine , salt metathesis reaction , combinatorial chemistry , reagent , peptide , disulfide bond , stereochemistry , organic chemistry , selenium , biochemistry , enzyme , polymerization , polymer
Peptides containing selenocysteine moieties are susceptible to non‐catalytic reactions of diselenide bonds metathesis induced by visible light. In contrast to previously reported radical metathesis of disulfide bridges in cysteine derivatives, this newly developed reaction is fast and clean, and proceeds without decomposition of peptides and without formation of side products. The diselenide bond in peptides was reported in literature to be more stable than the disulfide one and also less susceptible to metathesis induced by thiols and reducing reagents. We demonstrated that visible light induces fast metathesis of Se−Se bonds in peptides. This reaction is important for the folding of peptides containing selenocysteine residues and may find application in designing dynamic combinatorial libraries of peptides responsive to external influence.