期刊
FOOD CHEMISTRY
卷 242, 期 -, 页码 505-512出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.09.092
关键词
Curcumin; Intermolecular interaction; Analytical technique; BSA conformation; Photodegradation
资金
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Fundacao de Apoio a Pesquisa de Minas Gerais (FAPEMIG)
Bovine 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 10(5)L.mol(-1) by fluorescence and microcalorimetric, and 10(3) and 10(4) 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 (Delta H-F(Omicron) = -8.67 kJ.mol(-1)), while microcalorimetry showed an entropic driven binding process (Delta H-cal(Omicron) = 29.11 kJ.mol(-1)). For the unfolded BSA/curcumin complex, it was found thatp Delta H-F(Omicron) = -16.12 kJ.mol(-1) and Delta H-cal(Omicron) = -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.
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