Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins

CELEJ, M.S.; DASSIE SA,; GONZALEZ M,; BIANCONI ML,; FIDELIO G.D.

ACADEMIC PRESS INC ELSEVIER SCIENCE

Año: 2006 vol. 350 p. 277 - 277

p class="abstract">The stability of proteins and their interactions with other molecules is a topic of special interest in biochemistry because many cellular processes depend on that. New methods and approaches are constantly developed to elucidate the energetics of biomolecular recognition. In this sense, the application of the theory of macromolecular unfolding linked to ligand binding to differential scanning calorimetry (DSC) has proved to be a useful tool to simultaneously characterize the energetics of unfolding and binding. Although the general theory is well known, the applicability of DSC to study the interaction of biomolecules is not common. In the current work, we estimated the binding parameters of 8-anilinonaphthalene-1-sulfonic acid to human serum albumin using DSC. This model system was chosen due to both the complex stoichiometry and the moderate binding constants. From DSC curves acquired at different ligand concentrations, we obtained the number of bound ligands, th