Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.
Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, Leu- Gly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, Gly- Pro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The IC50 values of each tripeptide. namely Leu-Gly-Pro, Gly- Leu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu. were 0.72, 1.62, 2.65, 4.74, 5.73, and 13.93 microM, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as Gly- Pro and Pro-Leu with IC50 values of 252.6 and 337.3 microM, respectively. Among the tripeptides, Leu-Gly-Pro and Gly- Leu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.
Byun
Hee-Guk
HG
Department of Chemistry, Pukyong National University, Pusan 608-737, Korea.
Kim
Se-Kwon
SK
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D005399:Fishes; D066298:In Vitro Techniques; D008956:Models, Chemical; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry; D012867:Skin / Q000737:chemistry
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; D007703:Peptidyl-Dipeptidase A