Recent studies into the binding and inhibition of simian virus 40 large T-antigen (sv40-Tag) by deep-cavity cavitand octa-acid (OA) will be presented. Additionally, we will discuss the synthetic route to the cavitand utilized in our study. The protein described herein is a replicative helicase and exhibits the toroidal hexamer structure, which appears uniquely suited as a host to orient around the cavitand described in our study (fig. 1)We will focus on a series of fluorescent and absorbance assays, which have shown potential inhibition of the ATPase activity of sv40-Tag at �M concentrations of OA. We posit, based on MOE docking simulations, that OA orients towards several His, and Arg residues in the central Tag channel resulting in protein inhibition (fig. 2) We will further discuss the potential for assay interference and the possibility for OA serving as a host to bind other assay components. We will conclude with new directions for further work and possible implications.

Protein inhibition by a deep-cavity cavitand

248th National Meeting (2014)

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