Human Serum Albumin (HSA), a major protein component of plasma plays a major role as the principal cellular transporter in blood and is a major fatty acid binding protein. It reversibly and covalently binds to a broad range of ligands. Differential Scanning Calorimeter (DSC) measures the difference in heat absorption for a biological sample relative to a buffer reference as a function of temperature, with a characteristic enthalpy, and entropy. Using DSC, the excess heat capacity was plotted as a function of temperature, yielding a plot with a Gaussian shape. This technique measured the thermal stability of biological molecules and complements other routine biochemical assays like mass spectrometry, gel electrophoresis, and immunoassays. The first part of this study showed that DSC thermogram analysis showed specific, reproducible signature plasma thermogram curve with a melting temperature of 62.5o to 63.5 oC. In this study, the shift in the binding of HSA was compared to various medications like Ibuprofen, Tylenol, Naproxen, and Amoxicillin. The potential clinical utility of these assays, shows that the thermal denaturation, stability, binding affinities of various known and unknown “medications” or ligands can be compared and quantified.

Binding of human serum albumin to various medications

256th National Meeting (2018)

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