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Solid‐phase acyl donor as a substrate pool in kinetically controlled protease‐catalysed peptide synthesis
Author(s) -
Eichhorn U.,
BeckPiotraschke K.,
Schaaf R.,
Jakubke H.D.
Publication year - 1997
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/(sici)1099-1387(199707)3:4<261::aid-psc103>3.0.co;2-y
Subject(s) - protease , chemistry , substrate (aquarium) , peptide , peptide synthesis , combinatorial chemistry , substrate specificity , stereochemistry , biochemistry , enzyme , biology , ecology
Recently we have demonstrated the advantage of solid‐ phase substrate pools mainly in equilibrium controlled protease‐catalysed peptide syntheses. The extension of this approach to protease‐catalysed acyl transfer reactions will be presented. The model reaction was systematically investigated according to both the influence of solid phases present in the system on enzyme activity as well as nucleophile concentration on peptide yield. The key parameter for obtaining high peptide yield via acyl transfer is the ratio between aminolysis and hydrolysis. We combined high nucleophile concentrations with solid‐phase acyl donor pools. This approach enabled us to supply ester substrate and nucleophile in equimolar amounts in a high‐density media without the addition of any organic solvent. Several multi‐functional di‐ to tetrapeptides were obtained in moderate to high yields. ©1997 European Peptide Society and John Wiley & Sons, Ltd.