Chum salmon trypsin-catalyzed peptide synthesis with inverse substrates as acyl donor components at low temperature

Abstract

Chum salmon trypsin-catalyzed peptide synthesis has been studied by using p-amidinophenyl esters of N α-( tert-butyloxycarbonyl)amino acid as the acyl donor components at 0°C. The reaction conditions were optimized for an organic solvent, pH, and concentration of the acyl acceptor. The method was shown to be successful as a general method for the synthesis of the peptide, and also useful for the preparation of peptides containing d-amino acids. The enzymatic hydrolysis of the resulting products was negligible.