Abstract
Food-derived angiotensin-converting enzyme inhibitory peptide (ACEIP) has an effect in supportive therapeutic on hypertension. Bovine serum albumin (BSA) as a model transporter protein to explore the interaction mechanisms with casein-hydrolyzed ACEIP Val-Ala-Pro (VAP) by multi-spectroscopic, biolayer interferometry (BLI), isothermal titration calorimetry (ITC), molecular docking, and molecular dynamics simulations. Multi-spectroscopic analysis showed that the non-covalent complexes formed by VAP and BSA resulted in decreased hydrophobicity and α-helix contents on BSA, revealing the unfolding of the BSA structure. BLI revealed the reversible binding process of BSA to VAP. ITC confirmed that the combination of VAP to BSA was a spontaneous process mainly driven by entropy. Molecular docking and molecular dynamic simulations showed that VAP was primarily bound in site II of BSA by hydrogen bonding, hydrophobic interactions, van der Waals force, and electrostatic force. This study provides a systematic method to reveal the structure–activity relationship of ACEIPs.
Published Version
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