title: Review stapling peptides using cysteine crosslinking.
abstract: 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.
authors.affiliation: Institute for Molecular Bioscience, the University of Queensland, Brisbane, QLD, 4072, Australia.
authors.forename: David P
authors.initials: DP
authors.lastname: Fairlie
authors.affiliation: Institute for Molecular Bioscience, the University of Queensland, Brisbane, QLD, 4072, Australia.
authors.forename: Aline
authors.initials: A
authors.lastname: Dantas de Araujo
mesh_terms: D003545:Cysteine / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry; D055550:Protein Stability
chemical_list: D010456:Peptides, Cyclic; D003545:Cysteine
keywords: S-alkylation; S-arylation; chemoselective reaction; cysteine conjugation; macrocyclization; peptide stapling; thiol-ene coupling; α-helix