The coupling efficiency in alpha-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.
α-Chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: incorporation of non-protein amino acids into peptides
α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donors instead of the conventional methyl ester in organicsolvents such as acetonitrile with low water content. This approach is useful for the incorporation of non-protein amino acids such as halogenophenylalanines into peptides.