Enzymatic synthesis of a CCK-4 tripeptide fragment
Abstract：Objective To synthesize a tripeptide derivative Phac-Met-Asp(OMe)-Phe -NH2, which is a fragment of the gastrin C-terminal tetrapeptide CCK-4, by enzymatic reaction. Methods Three free enzymes, α-chymotrypsin, papain and thermolysin from acyl donor Phac-Met-OCam was involved in three steps. The choice of appropriate enzymes and solvents was selected.Results All enzymatic reactions were obtained in reasonable yields (63%-92%). FAB-MS and FD-MS verified the correct molecular mass of the peptides. Conclusion Studies on the α-chymotrypsin catalyzed coupling reaction between Phac-Met-OCam and H-Asp(OMe)2 have focused on the low water content media. By papain catalyzed saponification of Phac-Met-Asp(OMe)2, α-methyl ester of aspartic acid is selectively hydrolyzed to retain β-methyl ester, and Phac-Met-Asp (OMe)-OH and H-Phc-NH2 can be coupled efficiently by thermolysin.
Keywords：enzymatic synthesispeptide bondgastrin CCK-4tripeptide derivative
Publication Date：2003-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：4( 289-292 )