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Chemoenzymatic synthesis of tripeptide Bz-RGD-(OEt)_2 was conducted in this study. First, the free dipeptide Gly-Asp was synthesized via a novel chemical method, wherein only %L%-aspartic acid was used and was followed by the esterification of Gly-Asp. The formation of the linkage between the third amino acid Bz-Arg-OEt and Gly-Asp-(OEt)_2 was completed by using the enzymatic method in organic media. The effects of several factors such as pH, the water content, triethylamine(TEA), the molar ratio of the substrates, and the reaction time on the yield of Bz-RGD-(OEt)_2 were examined. It was obtained that the optimum conditions for Bz-RGD-(OEt)_2 synthesis in an ethanol/Tris-HCl buffer system(volume ratio 93∶7) were as follows: pH=8.0; temperature, 30 ℃; reaction time, 7 h. The tripeptide yield was 75.2%.
Chemoenzymatic synthesis of tripeptide Bz-RGD- (OEt) _2 was conducted in this study. First, the free dipeptide Gly-Asp was synthesized via a novel chemical method, where only% L% -aspartic acid was used and was followed by the esterification of Gly-Asp. The formation of the linkage between the third amino acid Bz-Arg-OEt and Gly-Asp- (OEt) _2 was completed by using the enzymatic method in organic media. The effects of several factors such as pH, the water content, triethylamine (TEA), the molar ratio of the substrates, and the reaction time on the yield of Bz-RGD- (OEt) _2 were examined. It was obtained that the optimum conditions for Bz-RGD- (OEt) _2 synthesis in an ethanol / Tris-HCl buffer system (volume ratio 93: 7) were as follows: pH = 8.0; temperature, 30 ° C; reaction time, 7 h. The tripeptide yield was 75.2%.