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dc.creatorHudson, Eliara Acipreste-
dc.creatorPaula, Hauster Maximiler Campos de-
dc.creatorFerreira, Guilherme Max Dias-
dc.creatorFerreira, Gabriel Max Dias-
dc.creatorHespanhol, Maria do Carmo-
dc.creatorSilva, Luis Henrique Mendes da-
dc.creatorPires, Ana Clarissa dos S.-
dc.identifier.citationHUDSON, E. A. et al. Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding. Food Chemistry, [S.l.], v. 242, p. 505-512, Mar. 2018.pt_BR
dc.description.abstractBovine 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.pt_BR
dc.sourceFood Chemistrypt_BR
dc.subjectIntermolecular interactionpt_BR
dc.subjectAnalytical techniquept_BR
dc.subjectBovine serum albumin (BSA)pt_BR
dc.titleThermodynamic and kinetic analyses of curcumin and bovine serum albumin bindingpt_BR
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