Plasminogen Activator Inhibitor-1 (PAI-1) is a protease inhibitor involved in several biological processes, including fibrinolysis. Elevated plasma levels of PAI-1 have been associated with both acute diseases such as myocardial infarction and chronic disorders like cancer, atherosclerosis and type-2 diabetes mellitus. Recent work has shown that polyphenolic short chain compounds can be effective inhibitors of PAI-1. Here we use combined classical molecular mechanics and quantum mechanics methods to examine the interaction between PAI-1 and a series of polyphenolic inhibitors. Specifically, we consider a series of structurally related inhibitors that differ in the number and position of hydroxyl groups. The results shed light on the role hydroxyl groups play in determining the strength of interaction between inactivator and protein.

Examining the strength of interactions between PAI-1 and a series of structurally-related inactivators

248th National Meeting (2014)

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