D-Leu-L-Phe-containing dipeptide inhibitors of α-chymotrypsin – the role of the N- and C-termini in enzyme affinity

Abstract

Three new compounds (3-5) based on a dipeptide non-covalent inhibitor (1) of α-chymotrypsin have been synthesised and assayed against the serine protease α-chymotrypsin. The stability of the compounds to α-chymotrypsin catalysed hydrolysis has been measured. All three compounds were inactive with a retained stability to enzyme catalysed hydrolysis.