Serum albumins play an important role in the delivery and elimination of drugs, drug-metabolites, and toxins.  The protein has known binding interactions with a wide variety of molecules and ions and is known to undergo pH and ion-dependent conformational changes with discrete spectroscopic and calorimetric signatures.   Recent drug binding studies in our laboratory aimed at elucidating the energetics of molecular recognition of substituted warfarin has revealed that albumins are more stable in higher concentrations that approximate physiologic ranges in pure water solutions devoid of buffer components normally utilized to stabilize protein preparations.  Here we present, a combination of absorbance, fluorescence, and circular dichroism spectral data that are designed to articulate the solution conditions that influence protein stability, drug-binding, and aggregation behavior.  These results are discussed in the context of changes in the secondary and tertiary structures of albumins during irreversible temperature-induced unfolding in the presence and absence of substituted warfarins.<br/>

Combined fluorescence and circular dichroism spectroscopic investigations examining the influence of buffer components on the stability and solubility of free and warfarin-bound serum albumins

255th National Meeting (2018)

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