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

Chum salmon trypsin-catalyzed peptide synthesis has been studied by using p-amidinophenyl esters of N-alpha-(tert-butyloxycarbonyl)amino acid as the acyl donor components at 0 degreesC. 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. (C) 2000 Elsevier Science B.V. All rights reserved.