α-Amylase inhibition, anti-glycation property and characterization of the binding interaction of citric acid with α-amylase using multiple spectroscopic, kinetics and molecular docking approaches

The quest to suppress complications associated with diabetes mellitus is ever increasing, while food additives and preservatives are currently being considered play additional roles besides their uses in enhancement preservation. In the present study, protective prowess of a common preservative (citric acid, CA) against advanced glycation end-products (AGEs) formation its binding interaction mechanism α-amylase (AMY), an enzyme linked hyperglycemia management, were examined. Enzyme inhibition kinetics, intrinsic fluorescence, synchronous 3D fluorescence spectroscopies, ultraviolet–visible (UV–Vis) absorption spectroscopy, Fourier transform-infrared (FT-IR) thermodynamics, molecular docking analyses employed. Results obtained showed that citric acid decreased activity via mixed (IC50 = 5.01 ± 0.87 mM, Kic 2.42 Kiu 160.34 mM) suppressed AGEs 0.795 0.001 mM). free was quenched static high bimolecular quenching constant (Kq) (Ka) values. Analysis thermodynamic properties revealed AMY-CA complex spontaneously formed (ΔG < 0), entropy driven (TΔS > ΔH), involvement electrostatic forces. UV–Vis, FT-IR spectroscopies affirmed alterations native conformation due CA interaction. interacted His-101, Asp-197, His-299, Glu-233 within AMY active site. Our findings indicated could impair interact slow down starch hydrolysis; vital management type 2 complications.