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metadata.artigo.dc.title: Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding
metadata.artigo.dc.creator: Hudson, Eliara Acipreste
Paula, Hauster Maximiler Campos de
Ferreira, Guilherme Max Dias
Ferreira, Gabriel Max Dias
Hespanhol, Maria do Carmo
Silva, Luis Henrique Mendes da
Pires, Ana Clarissa dos S.
metadata.artigo.dc.subject: Curcumin
Intermolecular interaction
Analytical technique
Bovine serum albumin (BSA)
metadata.artigo.dc.publisher: Elsevier Mar-2018
metadata.artigo.dc.identifier.citation: HUDSON, 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.
metadata.artigo.dc.description.abstract: 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 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.
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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