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Replacement of the Acrid tert ‐Butylthiol and an Improved Isolation Protocol for Cysteine Lipidation on a Peptide or Amino Acid (CLipPA)
Author(s) -
Yang SungHyun,
Hermant Yann O. J.,
Harris Paul W. R.,
Brimble Margaret A.
Publication year - 2020
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201901696
Subject(s) - lipid anchored protein , chemistry , cysteine , peptide , amino acid , thiol , combinatorial chemistry , biochemistry , peptide synthesis , enzyme , apoptosis , autophagy
Lipidation is a key modification affecting the physiochemical properties of peptides and widely used in the design of drug candidates. Cysteine Lipidation on a Peptide or Amino Acid (CLipPA) enables rapid synthesis of a library of S‐lipidated peptides via a thiol‐ene reaction between a free sulfhydryl group on cysteine‐containing peptide and a vinyl ester bearing a lipid. Optimization of the CLipPA procedure was performed by replacing the malodorous tert ‐butylthiol and modifying the work‐up procedure to facilitate the analysis and isolation of lipopeptides.