Multi-spectroscopic approaches and molecular simulation research of the intermolecular interaction between the angiotensin-converting enzyme inhibitor (ACE inhibitor) benazepril and bovine serum albumin (BSA).

Benazepril, a common ACE inhibitor, widely used in the treatment of arterial hypertension and congestive heart failure. In this study, We evaluated the characteristics of the interaction between benazepril and BSA under the simulated physiological condition (pH7.4) through various spectroscopic and molecular docking methods. Fluorescence and absorption spectroscopy results showed benazepril quenched the intrinsic fluorescence of BSA through a combined dynamic and static quenching mechanism. The number of binding sites (n) and the binding constant (K) of benazepril-BSA complex were circa 1 and 6.81×10M at 298K, respectively, indicating that the binding affinity between benazepril and BSA was moderate. The displacement experiments confirmed that benazepril binding to the site I of BSA, which was quite in accordance with molecular docking. The values of the Gibbs free energy (ΔG), enthalpic change (ΔH) and entropic change (ΔS) were negative, verifying that van der Waals force and hydrogen bonding interaction played a predominant roles in the process of spontaneous bonding. Furthermore, a slight change of the conformation in BSA upon benazepril interaction was proved through SF, 3-DF and FTIR spectroscopy results.