Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: Structure–activity relationship

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion

“…Molecular docking simulations of this pentapeptide with tACE (PDB: 1086) were carried out to correlate the ACE inhibitory potential with the primary structure. Through such docking simulations, we have previously demonstrated that tripeptide inhibitors bind to the active site of tACE in a manner that mimics the binding of lisinopril (Jimsheena & Gowda, 2010). The binding of NAQRP to tACE and the interactions as given by the best pose was suggestive of a different binding mode.…”

“…Arachin was isolated and purity ascertained as described earlier (Jimsheena & Gowda, 2010). One gram of arachin was suspended in 5 ml of either 0.05 M Tris HCl, pH 7.8, 0.05 M Tris HCl, pH 8.2, 0.05 M Tris HCl or pH 7.5, 0.01 M HCl pH 2.0 for trypsin, chymotrypsin, pancreatin, pepsin (and human gastric juice) respectively and digested using an enzyme substrate ratio of 1, 2, 4, 6, 8 and 10% (w/w) at 37°C for 4 h. The pH of the reaction mixture was maintained at the optimum pH by addition of either 1 N NaOH or HCl.…”

“…The structure of the ligands were constructed and optimised using the public domain web server PepBuild as described earlier (Jimsheena & Gowda, 2010).…”

“…Docking, clustering and other validation exercises were performed as reported previously (Jimsheena & Gowda, 2010).…”

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

“…In the same context, Wu et al [56] have reported that TLS displayed a high ACEinhibitory activity with no direct interaction between the peptide and the Zn(II) atom. In addition, Jimsheena and Gowda [57] described that arachin ACE-inhibitory peptides did not directly coordinate with the Zn(II) atom, but, their interaction with His383, His387 and Glu411 promoted their inhibitory activity. In contrast, Ko et al [7] studies have shown that MEVFVP, a competitive ACE inhibitor peptide, could bind the enzymatic active site through a metal ion interaction (Zn701), H-bond interactions including Glu411, Arg522, Asn66, and a Pi interaction bond via the Tyr523.…”