FIDELIO GERARDO DANIEL
Artículos
Título:
Ligand-Indiced thermostability in proteins: thermodynamics análisis os ANS-albumin interaction.
Autor/es:
CELEJ MS,; DASSIE SA,; FREIRE E,; BIANCONI ML,; FIDELIO GD
Editorial:
Elselvier
Referencias:
Lugar: Aceptado; Año: 2005 vol. 1750 p. 122 - 122
Resumen:
span lang="en" style="font-size: 12pt; font-family: "Times New Roman";">A comparative thermodynamic study of the interaction of anilinonaphthalene sulfonate (ANS) derivatives with bovine serum albumin (BSA) was performed by using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The chemically related ligands, 1,8-ANS and 2,6-ANS, present a similar affinity for BSA with different binding energetics. The analysis of the binding driving forces suggests that not only hydrophobic effect but also electrostatic interactions are relevant, even though they have been extensively used as probes for non-polar domains in proteins. Ligand association leads to an increase in protein thermostability, indicating that both dyes interact mainly with native BSA. ITC data show that 1,8-ANS and 2,6-ANS have a moderate affinity for BSA, with an association constant of around 1-9x10(5) M(-1) for the high-affinity site. Ligand binding is disfavoured by conformation