To combat the high prevalence of diabetes mellitus, researchers have developed competitive inhibitory drugs for the digestive enzyme α-glucosidase. The most effective drugs to surface, Miglitol and Acarbose, also carry several adverse side effects. Many natural substrates have shown greater inhibition, but their method of inhibition remains unclear. We conducted in silico docking studies of naturally occurring inhibitors that have shown, in literature, to rival IC50 values of current drugs. A series of flavonoids displayed high binding affinity to a possible allosteric pocket located adjacent to the active site. Our current focus is to complete in vitro inhibition assays of the flavonoids with high binding affinity. Then, the IC50 values will be correlated with the binding scores to help verify the proposed binding site. From this work, a map of the putative binding site and reactivity of the flavonoids can be produce.

In vivo inhibition of S. cerevisiae α-glucosidase validates molecular modeling and in silico inhibitor docking studies

255th National Meeting (2018)

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