Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry.

Differential scanning calorimetry has been used to study the thermal stability of bovine serum albumin as affected by binding of fatty acids (lauric acid and stearic acid) and sodium dodecyl sulfate (SDS). All the ligands stabilized the protein molecules in a similar manner, but to different levels. A maximum increase in denaturation temperature of 30 degrees C was obtained with lauric acid. The thermograms indicate the presence of several ligand-albumin complexes having different heat stabilities. Variations in pH in 0.9% NaCl affected the heat stability of both ligand-poor and ligand-rich albumin, the former being more sensitive to variations in pH within the physiological range. Variations in NaCl concentration affected the thermal stabilities at neutral pH, expecially at low salt concentrations. While ligand-rich albumin was somewhat destabilized by increasing NaCl concentrations, ligand-poor albumin was strongly stabilized. The potential use of differential scanning calorimetry in ligand-albumin research is discussed.