α-Chymotrypsin-catalysed peptide synthesis using activated esters as acyl donors
The coupling efficiency in α-chymotrypsin-catalysed peptide synthesis is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donor instead of the conventional methyl ester; this approach is useful for the incorporation of non-protein amino acids into peptides.
Porcine Pancreatic Lipase Catalyzed Enantioselective Hydrolysis of Esters of N-Protected Unusual Amino Acids
Porcine pancreatic lipase catalyzed the highly enantioselective hydrolysis of a kind of α-substituted carboxylic esters, i.e., the 2,2,2-trifluoroethyl esters of the N-benzyloxycarbonyl derivatives of unusual amino acids.