Gene

Alloxan

Acarbose

Amylase

Endocrinology

Biochemistry

Taxifolin

Antioxidant

Enzyme

Postprandial

Internal medicine

Pharmacology

Flavonoid

Medicine

Chemistry

In silico

Diabetes mellitus

Journal of Cellular Biochemistry

There has been a dramatic increase in the prevalence of diabetes mellitus (DM) and its associated complications globally. The postprandial stage of DM involves prompt elevation in the levels of blood glucose and α‐amylase, a carbohydrate‐metabolizing enzyme is mainly involved in the regulation of postprandial hyperglycemia. This study was designed to assess the ability of a well‐known flavonoid, taxifolin (TFN), against postprandial hyperglycemia and its inhibitory effects on α‐amylase activity through the assessment of therapeutic potentials of TFN in an alloxan‐induced diabetic animal model. The binding potential TFN with an α‐amylase receptor was also investigated through molecular dynamics (MD) simulation and docking of to compare the binding affinities and energies of TFN and standard drug acarbose (ACB) with target enzyme. TFN significantly improved the postprandial hyperglycemia, lipid profile, and serum levels of α‐amylase, lipase, and C‐reactive protein in a dose‐dependent manner when compared with that of either DM‐induced and ACB‐treated alloxan‐induced diabetic rats. Moreover, TFN also enhanced the anti‐oxidant status and normal functioning of the liver in alloxan‐induced diabetic rats more efficiently as compared to that of ACB‐treated alloxan‐induced diabetic rats. Therapeutic potentials of TFN were also verified by MD simulation and docking results, which exhibited that the binding energy and affinity of TFN to bind with receptor was significantly higher as compared to that of ACB. Hence, the results of this study signify that TFN might be a potent inhibitor of α‐amylase that has the potential to regulate the postprandial hyperglycemia along with its anti‐inflammatory and anti‐oxidant properties during the treatment of DM.

Taxifolin prevents postprandial hyperglycemia by regulating the activity of α‐amylase: Evidence from an in vivo and in silico studies