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. 2020 Jul 1;154:217-232.
doi: 10.1016/j.ijbiomac.2020.03.090. Epub 2020 Mar 12.

Exploring Efficacy of Indole-Based Dual Inhibitors for α-Glucosidase and α-Amylase Enzymes: In Silico, Biochemical and Kinetic Studies

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Exploring Efficacy of Indole-Based Dual Inhibitors for α-Glucosidase and α-Amylase Enzymes: In Silico, Biochemical and Kinetic Studies

Abdel-Nasser Kawde et al. Int J Biol Macromol. .

Abstract

α-Glucosidase and α-amylase are enzymes which are associated with diabetic II. These enzymes break macromolecules of sugar into monosugar molecules which is soluble in body, hence increase the sugar level in blood. There is need to develop economical and save inhibitors to prevent them from breaking sugar macromolecules to soluble molecules which will control the level of sugar in blood. Therefore, we synthesized indole-based derivatives (1-18) and evaluated as dual inhibitor for α-glucosidase and α-amylase. These chemical scaffolds were built with variation in aryl ring which were found active with good to moderate activity for α-glucosidase having IC50 value ranging from 13.99 ± 0.10 to 59.09 ± 0.30 μM when compared with standard acarbose with IC50 of 11.29 ± 0.10 μM; for α-amylase IC50 value ranging from 13.14 ± 0.10 to 58.99 ± 0.30 μM when compared with the standard acarbose with IC50 of 11.12 ± 0.10 μM. Structure activity relationship (SAR) has been established for all compounds. Enzymatic kinetic study and molecular docking study have been carried out to investigate the binding interactions α-glucosidase and α-amylase enzyme.

Keywords: Enzymatic kinetic study; Indole; Molecular docking; α-Amylase; α-Glucosidase.

Conflict of interest statement

Declaration of competing interest The authors declare no competing financial interests.

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