Investigations Using Molecular Docking and Simulation on the Antidiabetic Activity of Resveratrol Aldehyde Molecule.
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Abstract
Introduction: Diabetes mellitus (DM) is a heterogeneous group of disorders essentially characterized by variable degrees of impaired secretion (T1DM) and/or action of insulin (T2DM), leading to persistent elevation in blood glucose levels. T2DM is the most prevalent form, with an incidence of 90–95% of all known cases in the population. Due to the development of undesirable side effects associated with the currently prescribed drugs for the treatment of T2DM, the search for novel drugs continues.
Objectives: In the present study, we have investigated the in silico interactions of four proteins with synthesized resveratrol aldehyde.
Methods: Molecular docking is one of the most accepted and successful structure-based in silico methods, which facilitates predicting the interactions taking place between molecules and biological targets. Peripheral tissue resistance to insulin action, the characteristic feature of T2DM, is known to affect the metabolism of glucose and fat in humans. Several reports suggest that AMP-activated protein kinase, C-reactive protein (CRP), protein tyrosine phosphatase, and glutamine fructose-6-phosphate amidotransferase all play significant roles in the initiation, progression, and onset of T2DM.
Results: All four proteins exhibit a strong affinity for the resveratrol aldehyde. All the proteins, namely, Glutamine fructose-6-phosphate amidotransferase (ΔG:-7.24 kcal/mol), AMP:Activated protein kinase (ΔG:-7.23 kcal/mol), C-Reactive Protein (CRP) (ΔG:-7.11 kcal/mol), and Protein Tyrosine Phosphatase (PTP) (ΔG: -7.38 kcal/mol), showed strong binding affinities with resveratrol aldehyde.
Conclusions: Protein tyrosine phosphatase was a better lead molecule than other proteins, according to the results of the Molecular Docking simulation. Before demonstrating their therapeutic implications against diabetes, through, comprehensive wet-lab validations are necessary.