Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking.
| Autor: | Avwioroko OJ; Department of Biochemistry, Faculty of Basic Medical Sciences, Redeemer's University, Ede, Osun State, Nigeria.; Centre for Chemical and Biochemical Research (CCBR), Redeemer's University, Ede, Osun State, Nigeria., Oyetunde TT; Department of Chemical Sciences, Faculty of Natural Sciences, Redeemer's University, Ede, Osun State, Nigeria.; Centre for Chemical and Biochemical Research (CCBR), Redeemer's University, Ede, Osun State, Nigeria., Atanu FO; Department of Biochemistry, Faculty of Natural Sciences, Kogi State University, Anyigba, Nigeria., Otuechere CA; Department of Biochemistry, Faculty of Basic Medical Sciences, Redeemer's University, Ede, Osun State, Nigeria.; Centre for Chemical and Biochemical Research (CCBR), Redeemer's University, Ede, Osun State, Nigeria., Anigboro AA; Department of Biochemistry, Faculty of Science, Delta State University, Abraka, Nigeria., Dairo OF; Department of Physical Sciences, Faculty of Natural Sciences, Redeemer's University, Ede, Osun State, Nigeria., Ejoh AS; Department of Biological Sciences, Covenant University, Ota, Ogun State, Nigeria., Ajibade SO; Department of Chemical Sciences, Faculty of Natural Sciences, Redeemer's University, Ede, Osun State, Nigeria.; Centre for Chemical and Biochemical Research (CCBR), Redeemer's University, Ede, Osun State, Nigeria., Omorogie MO; Department of Chemical Sciences, Faculty of Natural Sciences, Redeemer's University, Ede, Osun State, Nigeria.; Centre for Chemical and Biochemical Research (CCBR), Redeemer's University, Ede, Osun State, Nigeria.; Water Science and Technology Research Unit, African Centre of Excellence for Water and Environmental Research (ACEWATER), Redeemer's University, Ede, Osun State, Nigeria. |
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| Jazyk: | angličtina |
| Zdroj: | Biochemistry and biophysics reports [Biochem Biophys Rep] 2020 Nov 14; Vol. 24, pp. 100837. Date of Electronic Publication: 2020 Nov 14 (Print Publication: 2020). |
| DOI: | 10.1016/j.bbrep.2020.100837 |
| Abstrakt: | 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. 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. The ligands were characterized using 1 H and 31 P NMR spectroscopy and CHN analysis. 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 -1 s -1 , indicating formation of enzyme-ligand complexes. A binding stoichiometry of n≈1 was observed for α-amylase, with high binding constants (Ka). α-Amylase inhibition was as follow: Acarbose > DY301>DY300>DY302. 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). UV-visible spectroscopy and Förster resonance energy transfer (FRET) affirmed change in enzyme conformation and binding occurrence. Molecular docking revealed ligands interaction with α-amylase via some key catalytic site amino acid residues (Asp197, Glu233 and Asp300). DY301 perhaps showed highest α-amylase inhibition (IC Competing Interests: The authors declare no conflict of interests. (© 2020 The Authors.) |
| Databáze: | MEDLINE |
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