Preparation, identification, and molecular docking of novel elastase inhibitory peptide from walnut (Juglans regia L.) meal.

ABSTRACT: This study aimed to isolate bioactive peptides with elastase inhibitory activity from walnut meal via ultrasonic enzymatic hydrolysis. The optimal hydrolysis conditions of walnut meal protein hydrolysates (WMPHs) were obtained by response surface methodology (RSM), while a molecular weight of<3 kDa fraction was analyzed by LC-MS/MS, and 556 peptides were identified. PyRx virtual screening and Autodock Vina molecular docking revealed that the pentapeptide Phe-Phe-Val-Pro-Phe (FFVPF) could interact with elastase primarily through hydrophobic interactions, hydrogen bonds, and π-sulfur bonds, with a binding energy of -5.22 kcal/mol. The verification results of inhibitory activity showed that FFVPF had better elastase inhibitory activity, with IC₅₀ values of 0.469 ± 0.01 mg/mL. Furth

SUBMITTER: Xiong Y 

PROVIDER: S-EPMC9574760 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature