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- W2279047369 abstract "Alpha-glucosidase is intestinal enzyme which catalyzes the degradation of diet polysaccharides to absorbable monosaccharide. Natural or synthetic glucosidase inhibitors are of therapeutic interest to delay postprandial hyperglycemia in type 2diabetes.The objective of this investigation was to characterize and determine the effect of the natural compounds on α-Glucosidase which is an important protein involved in Type 2 Diabetes. Homology modeling of a Glucosidase (Human) has been performed based on the crystal structure of the 2QLY by using Modeller software. With the aid of the molecular mechanics and molecular dynamics methods, the final model is obtained and is further assessed by procheck and verify 3D graph programs, which showed that the final refined model is reliable. With this model, a flexible docking study of α-Glucosidase with a group of natural compounds which were selected from the previous publications was performed. The results indicated that TYR77, VAL78, A5N82, ILE83, GLUI02 in α-Glucosidase are important determinant residues in binding as they have strong hydrogen bonding with compounds. These hydrogen binding interactions play an important role for stability of the complex. Among the compounds docked, Acarbose showed best docking result with P-glycoprotein. Our results may be helpful for further experimental investigations." @default.
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- W2279047369 date "2010-01-01" @default.
- W2279047369 modified "2023-09-23" @default.
- W2279047369 title "Homology modeling and docking studies of alpha glucosidase involved in type 2 diabetes" @default.
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