Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking
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 dichalcoge...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | Biochemistry and Biophysics Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580820301473 |
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| author | Oghenetega J. Avwioroko Temidayo T. Oyetunde Francis O. Atanu Chiagoziem A. Otuechere Akpovwehwee A. Anigboro Oluropo F. Dairo Akpoyovware S. Ejoh Sunday O. Ajibade Martins O. Omorogie |
| author_facet | Oghenetega J. Avwioroko Temidayo T. Oyetunde Francis O. Atanu Chiagoziem A. Otuechere Akpovwehwee A. Anigboro Oluropo F. Dairo Akpoyovware S. Ejoh Sunday O. Ajibade Martins O. Omorogie |
| author_sort | Oghenetega J. Avwioroko |
| collection | DOAJ |
| description | 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 1H and 31P 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 x1011 M-1s-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 (IC50, 268.11 ± 0.74 μM) due to its moderately high affinity and composition of two sulphide bonds unlike the others. This study might provide theoretical basis for development of novel α-amylase inhibitors from dichalcogenoimidodiphosphinate ligands for management of postprandial hyperglycemia. |
| first_indexed | 2024-12-16T15:34:38Z |
| format | Article |
| id | doaj.art-3731b1ed9cf94471a919c964dfae4022 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-16T15:34:38Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
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| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-3731b1ed9cf94471a919c964dfae40222022-12-21T22:26:15ZengElsevierBiochemistry and Biophysics Reports2405-58082020-12-0124100837Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular dockingOghenetega J. Avwioroko0Temidayo T. Oyetunde1Francis O. Atanu2Chiagoziem A. Otuechere3Akpovwehwee A. Anigboro4Oluropo F. Dairo5Akpoyovware S. Ejoh6Sunday O. Ajibade7Martins O. Omorogie8Department 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; Corresponding author. Department of Biochemistry, Faculty of Basic Medical Sciences, Redeemer’s University, Ede, Osun State, Nigeria.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, NigeriaDepartment of Biochemistry, Faculty of Natural Sciences, Kogi State University, Anyigba, NigeriaDepartment 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, NigeriaDepartment of Biochemistry, Faculty of Science, Delta State University, Abraka, NigeriaDepartment of Physical Sciences, Faculty of Natural Sciences, Redeemer’s University, Ede, Osun State, NigeriaDepartment of Biological Sciences, Covenant University, Ota, Ogun State, NigeriaDepartment 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, NigeriaDepartment 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, NigeriaPostprandial 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 1H and 31P 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 x1011 M-1s-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 (IC50, 268.11 ± 0.74 μM) due to its moderately high affinity and composition of two sulphide bonds unlike the others. This study might provide theoretical basis for development of novel α-amylase inhibitors from dichalcogenoimidodiphosphinate ligands for management of postprandial hyperglycemia.http://www.sciencedirect.com/science/article/pii/S2405580820301473α-Amylase inhibitionLigand-protein bindingSpectroscopyHyperglycemiaAnti-diabetic agents |
| spellingShingle | Oghenetega J. Avwioroko Temidayo T. Oyetunde Francis O. Atanu Chiagoziem A. Otuechere Akpovwehwee A. Anigboro Oluropo F. Dairo Akpoyovware S. Ejoh Sunday O. Ajibade Martins O. Omorogie Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking Biochemistry and Biophysics Reports α-Amylase inhibition Ligand-protein binding Spectroscopy Hyperglycemia Anti-diabetic agents |
| title | Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking |
| title_full | Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking |
| title_fullStr | Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking |
| title_full_unstemmed | Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking |
| title_short | Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking |
| title_sort | exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α amylase spectroscopic approach coupled with molecular docking |
| topic | α-Amylase inhibition Ligand-protein binding Spectroscopy Hyperglycemia Anti-diabetic agents |
| url | http://www.sciencedirect.com/science/article/pii/S2405580820301473 |
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