Fractionation and Identification of Bioactive Peptides from Camel Skin Hydrolysate: In Silico and Molecular Docking Analysis

Abstract

Hypertension and glycemia disorders are severe issues in public health, highlighting the urgent need for the discovery of natural bioactive agents with health benefits. In this sense, the present study examines camel skin gelatin hydrolyzate, obtained using Alcalase (GHA). GHA was first ultrafiltrated, and the low molecular weight fraction (<10 kDa) with the highest in vitro ACE and DPP-IV inhibitory activities (82.75% and 72.5%, respectively) was further purified by reversed-phase high-performance liquid chromatography. Among the resulting fractions (FI to FV), FIII and FIV were the most potent inhibitors against the ACE activity. Thus, they were analyzed by LC-MS/MS for peptide identification. In silico and peptidomic analyses revealed several novel peptide sequences. Molecular docking and MM-GBSA studies were subsequently performed to investigate the interactions and estimate the binding energies of the selected peptides with ACE and DPP-IV. Among the investigated peptides, GPSGPSGL and GPSGPR showed the strongest energy-binding scores against the studied enzymes with favorable interactions with their active sites. In conclusion, hydrolyzed camel skin gelatin is a promising source of multifunctional bioactive peptides and a potential natural ingredient for the management of hypertension and glycemic disorders.