Hudson, Eliara AciprestePaula, Hauster Maximiler Campos deFerreira, Guilherme Max DiasFerreira, Gabriel Max DiasHespanhol, Maria do CarmoSilva, Luis Henrique Mendes daPires, Ana Clarissa dos Santos2019-05-032019-05-032018HUDSON, E. A. et al. Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding. Food Chemistry, v. 242, p. 505-512, mar. 2018. Disponível em: <https://www.sciencedirect.com/science/article/pii/S0308814617315674?via%3Dihub>. Acesso em: 7 mar. 2019.0308-8146http://www.repositorio.ufop.br/handle/123456789/11182Bovine serum albumin (BSA)/curcumin binding and dye photodegradation stability were evaluated. BSA/curcumin complex showed 1:1 stoichiometry, but the thermodynamic binding parameters depended on the technique used and BSA conformation. The binding constant was of the order of 105 L·mol−1 by fluorescence and microcalorimetric, and 103 and 104 L·mol−1 by surface plasmon resonance (steady-state equilibrium and kinetic experiments, respectively). For native BSA/curcumin, fluorescence indicated an enthalpic and entropic driven process based on the standard enthalpy change (ΔH○F = −8.67 kJ·mol−1), while microcalorimetry showed an entropic driven binding process (ΔH○cal = 29.11 kJ·mol−1). For the unfolded BSA/curcumin complex, it was found thatp ΔH○F = −16.12 kJ·mol−1 and ΔH○cal = −42.63 kJ·mol−1. BSA (mainly native) increased the curcumin photodegradation stability. This work proved the importance of using different techniques to characterize the protein-ligand binding.en-USrestritoIntermolecular interactionAnalytical techniqueBSA conformationPhotodegradationArtigo publicado em periodicohttps://www.sciencedirect.com/science/article/pii/S0308814617315674https://doi.org/10.1016/j.foodchem.2017.09.092