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Trypsin‐catalysed synthesis of oligopeptide amides: comparison of catalytic efficiency among trypsins of different origin (bovine, streptomyces griseus and chum salmon)
Author(s) -
Sekizaki Haruo,
Itoh Kunihiko,
Toyota Eiko,
Tanizawa Kazutaka
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.406
Subject(s) - streptomyces griseus , amide , oligopeptide , chemistry , trypsin , pentapeptide repeat , enzyme , streptomyces , amino acid , biochemistry , catalysis , peptide , stereochemistry , combinatorial chemistry , biology , bacteria , genetics
A procedure has been developed for the synthesis of oligopeptide amide using inverse substrates as acyl donors with amino acid amide instead of p ‐nitroanilide as acyl acceptor and trypsins of different origin (bovine, Streptomyces griseus and chum salmon trypsins) as the catalyst. The effectiveness of this procedure was demonstrated by the synthesis of a pentapeptide, Boc‐[Leu 5 ]‐enkephalin amide, as a model compound. The method was the first enzymatic method shown to be successful at each successive coupling step for the synthesis of the oligopeptide. Bovine and chum salmon trypsins were superior to Streptomyces griseus trypsin as the catalyst. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.