Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

Abstract

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, LeuGly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, GlyPro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The IC 50 values of each tripeptide − namely Leu-Gly-Pro, GlyLeu-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 µM, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as GlyPro and Pro-Leu with IC 50 values of 252.6 and 337.3 µM, respectively. Among the tripeptides, Leu-Gly-Pro and GlyLeu-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.

Structural Characteristics and Antihypertensive Effects of Angiotensin-Iconverting Enzyme Inhibitory Peptides in the Renin-Angiotensin and Kallikrein Kinin Systems

“…The zinc ion of ACE is correctly positioned between S1 and S1' to contribute in the hydrolytic cleavage of the substrate peptide bond causing the release of the dipeptide product. ACE active sites S1, S1'and S2' have high attractions for the side chains of tryptophan, alanine, and proline, respectively (Byun & Kim, 2002). Therefore, it can be concluded that ACE seems to favour substrates or competitive inhibitors that comprise hydrophobic amino acid residues at the three locations of the C-terminal which will interact with these subsites (Hong et al, 2008).…”

ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

“…The C -terminal tripeptide residues may interact with the subsites S1, S1' , and S2' at the active site of ACE. ACE appears to prefer substrates or competitive inhibitors that contain hydrophobic amino acid residues at the three positions of the C -terminal (Byun & Kim, 2002). Matsumura et al (1993) isolated four ACE inhibitory peptides from an autolysate of bonito bowels.…”

“…According to Byun & Kim (2002). ACE inhibitory peptides that are derived from proteins are regarded as competitive substrates for ACE.…”

Biologically Active Peptides Released From Food Proteins

“…[82] wykazali, że niektóre białka jaja kurzego mogą być dobrym źródłem peptydów redukujących ciśnienie krwi. Przykła-dem jest owoalbumina, w której zidentyfikowano następujące peptydy przeciwnadciśnieniowe: YAEERYPIL (31,6), IVF (31,7), RADHPFL (34,0) [65], RADHP (25,0) [64], FRADHPFL (18,0), RADHPF (10,6), LW (22,0) [58]. W nawiasach podano poziom redukcji ciśnienia tętniczego krwi u szczurów w mm Hg.…”

“…Dawka 0,15 g tego hydrolizatu na kilogram masy ciała obniżała ciśnienie krwi u szczurów [61]. Źródłem peptydów inhibitorów ACE są także α-zeina kukurydzy [6], karboksylaza rybulozo-1,5-bisfosforanu [E.C. 4.1.1.39] (in.…”