Insights into the Inhibition Mechanism of Human Pancreatic α-Amylase, a Type 2 Diabetes Target, by Dehydrodieugenol B Isolated from <i>Ocimum tenuiflorum</i>
Prasad D. Dandekar, Amol S. Kotmale, Shrawan R. Chavan, Pranita P. Kadlag, Sangeeta Sawant, Dilip D. Dhavale, Ameeta RaviKumar
Abstract
) of 0.507 μM. Molecular docking showed stable HPA-inhibitor binding involving H-bonds and Pi-alkyl, alkyl-alkyl, and van der Waals (vDW) interactions. The computational docking results support the noncompetitive nature of DDEB binding. The present study could be helpful for exploration of the molecule as a potential antidiabetic drug candidate to control postprandial hyperglycemia.
Topics & Concepts
Isothermal titration calorimetryChemistryCircular dichroismDissociation constantvan der Waals forceDocking (animal)Binding constantPostprandialMixed inhibitionStereochemistryBinding siteCrystallographyMoleculeBiochemistryEnzymeNon-competitive inhibitionOrganic chemistryInsulinBiologyMedicineNursingReceptorEndocrinologyNatural Antidiabetic Agents StudiesEnzyme Production and CharacterizationComputational Drug Discovery Methods