Identification, in silico screening, and molecular docking of novel ACE inhibitory peptides isolated from the edible symbiot Boletus griseus-Hypomyces chrysospermus

• Published in: Food science & technology Vol. 169; p. 114008
• Main Authors: Renjuan, Li, Xiuli, Zhou, Liping, Sun, Yongliang, Zhuang
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.11.2022
• Subjects: absorption; ACE inhibitory Peptide; active sites; Boletus; computer simulation; computer software; enzymes; excretion; hydrogen; hydrophobicity; In silico screening; metabolism; methanol; Molecular docking; peptides; tandem mass spectrometry; ultra-performance liquid chromatography; In silico screening; ACE inhibitory Peptide; Molecular docking
• ISSN: 0023-6438
• DOI: 10.1016/j.lwt.2022.114008

The aim of this study is to find angiotensin-Ⅰ-converting enzyme inhibitory (ACEI) peptides from the edible symbiot Boletus griseus-Hypomyces chrysospermus (BGHC). The peptides from the methanol extract of BGHC were identified through ultraperformance liquid chromatography quadrupole Orbitrap tandem mass spectrometry analysis coupled with de novo sequencing by using Peak Studio software. Subsequently, two ACEI peptides, being KYPHVF and LFRPE, were screened on the basis of PeptideRanker and the AHTpin online server. The in silico absorption, distribution, metabolism, excretion and toxicities (ADMET) of the two peptides were predicted with AdmetSAR software, and the two peptides showed good absorption and nontoxicity. Meanwhile, the ACEI mechanism of KYPHVF and LFRPE was analyzed through molecular docking with SYBYL-X 2.0 software. The molecular docking study revealed that the total scores of the interactions of KYPHVF and LFRPE with ACE were 12.53 and 11.34, respectively. KYPHVF and LFRPE could establish hydrogen bonds and hydrophobic interactions with the active site of ACE. Furthermore, the ACEI activities of KYPHVF and LFRPE were determined in vitro with the IC50 values of 5.99 and 58.15 μmol/L, respectively. •KYPHVF and LFRPE were screened from Boletus griseus-Hypomyces chrysospermu.•Two peptides showed high ACE inhibitory activity in silico.•Two peptides formed hydrogen bonds and hydrophobic interactions with ACE.•The IC50 values of ACEI activity of two peptides were 5.99 μM and 58.15 μM.