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Updated: Aug 12, 2026

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
Published on: June 20, 2014
Preparation of carboxyl-terminal tryptic peptides from proteins by cleavage at arginine
Abstract:
A method has been developed for selectively preparing the carboxyl-terminal tryptic peptide of proteins by cleavage at arginyl residues. The succinylated protein is digested with trypsin and the peptides produced are maleylated. Maleylated peptides are then submitted to cation-exchange chromatography in urea at low pH and ionic strength. Arginine-containing peptides are retained by the resin. The carboxyl-terminal peptide emerges unretarded and in pure form. This method has been applied to four proteins of known sequence. Yields as high as 88% have been obtained.
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