Due to the increasing problem of diabetes mellitus throughout the world, research on digestive enzymes such as α-glucosidase has become more prevalent. The identification of the active site in α-glucosidase has led to competitive inhibitory drugs such as Miglitol and Acarbose. Many natural substrates have shown greater inhibition but their method of inhibition remains unclear. Our current focus is on docking natural substrates with published IC<sub>50</sub> values under 1 mM and evaluating their free energy and fit. Using a yeast α-glucosidase model, we have located seven potential binding pockets and the next steps in our research are to dock our compiled list of known inhibitors to each pocket to evaluate their fit. The amino acids participating in the H-bonding and π-π stacking will be mapped on the binding pockets, and the common structures of the best-docked inhibitors will be defined. By validating literature IC<sub>50</sub> values through structural analysis, we can help clarify the drug design pathway for α-glucosidase and diabetes mellitus.

Structural analysis of novel inhibitors through docking of homology modeled yeast α-glucosidase

253rd National Meeting (2017)

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