Advances in the structure determinations of serum albumin reveal that the binding of different ligands results in a shift in the number and type of salt-bridges resulting from the movements of amino acid side-chains throughout the protein structure. These side-chain movements occur mostly independently of the backbone, which is held in a relatively fixed conformation by 17 disulfide bonds. Here, we present results from a rigorous comparison of the various crystal structures of the protein formed in the presence and absence of various ligands including chloride anion, R- and S-warfarin, and fatty acids. We also present results from biophysical methods including solution differential scanning calorimetry (DSC), fluorescence spectroscopy, and UV-visible spectrophotometry, used to investigate the thermal stability of the protein. Molecular modeling and semi-empirical calculations provide insight into the differential stability of human serum albumin over a range of solution conditions and in the presence of various small molecule ligands.

Influence of amino acid side-chain mobility, drug binding, and disulfide bonding on the thermal stability of native human serum albumin

245th National Meeting (2013)

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