In the field of drug design, predicting interactions between a drug and its target-binding site is essential when evaluating drug candidates. However, in order to have an accurate prediction of these interactions, it is important to consider the role of water involved. Past studies have shown that the difference in hydration sensitivity between the quartz crystal microbalance and the dual polarization interferometer allows the instruments to be used in tandem to investigate changes in hydration states of protein-drug complexes. We sought to use this technique to understand and create a profile on how drugs of varying hydrophobicities alter the hydration state of bovine serum albumin. The degree of desolvation of drugs of varying hydrophobicities including Triflupromazine, Indomethacin, Procaine, and Labetalol was investigated. In general, drugs with higher hydrophobicities were shown to bind more tightly to their target site and displace more water molecules than hydrophilic drugs.

Quantifying desolvation of varying protein-drug complexes using the quartz crystal microbalance and dual polarization interferometer

245th National Meeting (2013)

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