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In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs

Published: Wednesday, April 03, 2013
Last Updated: Wednesday, April 03, 2013
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Binding of a drug molecule to HSA results in increased solubility in plasma, decreased toxicity, and protection against oxidation of the bound molecule.

Abstract
Since binding of a drug molecule to human serum albumin (HSA) significantly affects the pharmacokinetics of the drug, it is highly desirable to predict the binding affinity of the drug. Profen drugs are a widely used class of nonsteroidal anti-inflammatory drugs and it has been reported that several members of the profen class specifically bind to one of the main binding sites named site II. The actual binding mode of only ibuprofen has been directly confirmed by X-ray crystallography. Therefore, it is of interest whether other profen drugs are site II binders. Docking simulations using multiple template structures of HSA from three crystal structures of complexes between drugs and HSA have demonstrated that most of the currently available profen drugs should be site II binders.

This article was published online in ISRN Pahrmaceutics and is free to access.


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