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![]() ![]() DY301 perhaps showed highest α-amylase inhibition (IC 50, 268.11 ± 0.74 μM) due to its moderately high affinity and composition of two sulphide bonds unlike the others. Molecular docking revealed ligands interaction with α-amylase via some key catalytic site amino acid residues (Asp197, Glu233 and Asp300). UV–visible spectroscopy and Förster resonance energy transfer (FRET) affirmed change in enzyme conformation and binding occurrence. Values of thermodynamic parameters obtained at temperatures investigated (298, 304 and 310 K) revealed spontaneous complex formation (ΔG<0) between the ligands and α-amylase the main driving forces were hydrophobic interactions (with DY300, DY301, except DY302). α-Amylase inhibition was as follow: Acarbose > DY301>DY300>DY302. A binding stoichiometry of n≈1 was observed for α-amylase, with high binding constants (Ka). Diselenoimidodiphosphinate ligand (DY300), dithioimidodiphosphinate ligand (DY301), and thioselenoimidodiphosphinate ligand (DY302) quenched the intrinsic fluorescence intensity of α-amylase via a static quenching mechanism with bimolecular quenching constant (Kq) values in the order of x10 11 M -1s -1, indicating formation of enzyme-ligand complexes. The ligands were characterized using 1H and 31P NMR spectroscopy and CHN analysis. The present study investigated the binding interactions of three structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase to ascertain the affinity of the ligands for α-amylase using spectroscopic and molecular docking methods. Postprandial hyperglycemia has orchestrated untimely death among diabetic patients over the decades and regulation of α-amylase activity is now becoming a promising management option for type 2 diabetes. ![]()
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