Identification and molecular mechanism of angiotensin-convertingenzyme inhibitory peptides from Larimichthys crocea titin

This study aimed to identify novel ACEI peptides from Larimichthys crocea titin using in silico approachesand to clarify the molecular interaction mechanism. The hydrolyzed peptides of titin were comparedwith known ACEI peptides in the AHTPDB and BIOPEP-UWM database. Furthermore, peptides were eval-uated for their solubility, ADMET properties, Delta G (kcal/mol) values, and in vitro ACEI activity. Molecularmechanism of ACE-peptide was performed by molecular interactions and binding orientation study.The results revealed that IC50 values of Trp-Ala-Arg(WAR) and Trp-Gln-Arg(WQR) were (31.2 +/- 0.8) and(231.33 +/- 0.02) mu mol/L, respectively. The docking interactions result suggested that ACE-WAR and ACE-WQR complexes have same binding site, including the residues LYS511, TYR520, TYR523, HIS353, andHIS513. Molecular docking of two tripeptides WAR and WQR with ACE studies predicted their bindingsite and clarified the interaction between ACE and its inhibitors. The molecular docking data are consis-tent with the ACE inhibitory activity of the studied peptides. The results showed that Larimichthys croceatitin may be a valuable source for developing nutraceutical food.(c) 2020 Society information. Production and hosting by Elsevier B.V. on behalf of KeAiCommunications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/