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Stapling peptides using cysteine crosslinking
Author(s) -
Fairlie David P,
Dantas de Araujo Aline
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22877
Subject(s) - cysteine , chemistry , peptide , covalent bond , cyclic peptide , side chain , native chemical ligation , combinatorial chemistry , biochemistry , stereochemistry , organic chemistry , enzyme , polymer
Stapled peptides are an emerging class of cyclic peptide molecules with enhanced biophysical properties such as conformational and proteolytic stability, cellular uptake and elevated binding affinity and specificity for their biological targets. Among the limited number of chemistries available for their synthesis, the cysteine‐based stapling strategy has received considerable development in the last few years driven by facile access from cysteine‐functionalized peptide precursors. Here we present some recent advances in peptide and protein stapling where the side‐chains of cysteine residues are covalently connected with a range of different crosslinkers affording bisthioether macrocyclic peptides of varying topology and biophysical properties. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 843–852, 2016.