Angiotensin I-converting enzyme inhibitory oligo-tyrosine peptides synthesized by α-chymotrypsin

摘要: Abstract Oligo-tyrosine peptides with degrees of polymerization ranging from 2 to 5 could be synthesized by α-chymotrypsin-catalyzed reaction l -tyrosine ethyl ester in aqueous media, although the peptide yield was low due a preferential hydrolysis substrate. It also confirmed that α-chymotrypsin efficiently converted tyrosine tetramer dimer which resistant digestion. Both Tyr-Tyr and Tyr-Tyr-Tyr showed high inhibitory activity for angiotensin I-converting enzyme rabbit lung, their IC 50 values were 34 μM 51 μM, respectively. These two exhibited mix competitive noncompetitive inhibitions. first recognized as an ACE inhibitor, suggesting applied synthesis novel potential materials antihypertensive medicines.