Enzyme‐Catalyzed Peptide‐Bond Formation: Elastase‐ and δ‐Chymotrypsin‐Assisted Synthesis of Oligopeptides

A series of penta- and hexapeptides of the structure Ac-Lxn- …-Lx1-Ly1-…-Lym-NH2 with phenylalanine or tyrosine in Lx1 and glycine or alanine in the other positions were synthesized using elastase and δ-chymotrypsin to catalyse the formation of the peptide bonds adjacent to the aromatic residue. Such oligopeptides are useful substrates for studying the secondary specificity of chymotrypsin-like proteases.