Abstract
Glycogen phosphorylase (GP) is an important therapeutic target for type 2 diabetes having a direct influence on blood glucose levels through the glycogenolysis pathway. GP is an allosteric enzyme and with seven different binding sites discovered to date, there are multiple opportunities for modulation of its activity. Considerable efforts toward the design of drug-like GP inhibitors have taken place in recent years. Many of these inhibitors are natural products and their analogues. Focusing mainly on recent studies, this chapter will present the role that different in silico methods have played in their discovery.
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