Replacement of the Acrid <i>tert</i>‐Butylthiol and an Improved Isolation Protocol for Cysteine Lipidation on a Peptide or Amino Acid (CLipPA)
Sung‐Hyun Yang, Yann O. Hermant, Paul W. R. Harris, Margaret A. Brimble
Abstract
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.
Topics & Concepts
Lipid-anchored proteinChemistryCysteinePeptideAmino acidThiolCombinatorial chemistryBiochemistryPeptide synthesisEnzymeAutophagyApoptosisChemical Synthesis and AnalysisClick Chemistry and ApplicationsSulfur-Based Synthesis Techniques