ISSN:
1434-4475
Keywords:
Enzymic synthesis in biphasic systems
;
Peptide synthesis
;
α-Chymotrypsin
;
Papain
;
Thermolysin
;
Protected Eledoisin (6–11)-hexapeptide
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Papain and α-chymotrypsin were used for the protease-catalyzed assembly ofBoc-protected eledoisin (6−11)-hexapeptide by (2+4)- and (3+3)-segment condensation, respectively, in aqueous-organic solvent systems. As C-components, chemically synthesizedBoc-protected peptide methyl esters were employed. The nucleophilic tetrapeptide amide was prepared by papain-catalyzed (2+2)-segment coupling, while theZ-protected C-terminal dipeptide amide could be obtained by α-chymotrypsin- and thermolysin-catalyzed peptide bond formation. In addition, the influence of various reaction conditions, such as solvent composition, nucleophile concentration and reaction time, on the yield of theBoc-protected eledoisin (6−11)-hexapeptide was determined.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00810003
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