In silico and in vitro analysis of dipeptidyl peptidase-IV and angiotensin-converting enzyme inhibitory peptides derived from milk lactoferrin
Cherise Elisha, Prashant Bhagwat, Santhosh Pillai
Abstract
The study explores the inhibitory potential of bioactive peptides from lactoferrin (LF), a versatile milk glycoprotein derived from bovine and human milk, against angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV). Firstly, in silico digested LF sequences were screened for potential ACE and DPP-IV inhibitory activity using AHTpin and StackDPPIV, respectively. Molecular docking showed that bovine LF peptides, “EPYF” (−10.1 kcal mol −1 ) and “WQWR” (−9.3 kcal mol −1 ), had significantly lower binding energies with ACE and DPP-IV, respectively. In addition, in vitro analysis of bovine LF hydrolysates displayed an IC50 value of 0.48 ± 0.01 (ACE) and 0.93 ± 0.02 mg mL −1 (DPP-IV). Liquid chromatography-mass spectrometry (LC-MS/MS) analysis identified ACE and DPP-IV inhibitory peptides, “EPYF” and “WQWR”, which were present within the parent peptide sequences of the bovine LF hydrolysates. Considering the potential bioactivities of bovine LF peptides and their functional similarities with human LF, bovine LF could be exploited as a promising alternative to human LF.