Pepsin generated camel whey protein hydrolysates with potential antihypertensive properties: Identification and molecular docking of antihypertensive peptides

Abstract

This study reports the angiotensin converting enzyme (ACE) inhibiting potential of peptic camel whey hydrolysates (WHs) produced under different hydrolysis conditions. WHs displayed ACE inhibitory IC50 values in the range of 0.197–1.307 mg/mL. Among 27 hydrolysates generated, four, with the lowest IC50, were subjected to peptide sequencing using LC-MS QTOF and 185 different peptide sequences were identified. Peptides with a high PeptideRanker score (>0.8) were subsequently studied for possible interactions with ACE using in silico analysis. Based on the interaction of peptides with the hot-spots on the enzyme, PAGNFLP, FCCLGPVPP, PAGNFLMNGLMHR, and PAVACCLPPLPCHM were identified as potential ACE inhibitors. Molecular docking was also employed to identify how the shorter peptides interact in the active site of ACE. Furthermore, due to the importance of renin in managing hypertension, peptides from selected WHs with a potential to interact with renin were predicted using in silico analysis. Molecular docking was employed to predict how the identified peptides, PVAAAPVM and LRPFL, could interact with renin and potentially inhibit it. Thus, this study suggests that enzymatic hydrolysis of camel whey proteins could release peptides with potential anti-hypertensive properties.