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Title: Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding.
Authors: 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 Santos
Keywords: Intermolecular interaction
Analytical technique
BSA conformation
Issue Date: 2018
Citation: HUDSON, 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: <>. Acesso em: 7 mar. 2019.
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.
ISSN: 0308-8146
Appears in Collections:DEQUI - Artigos publicados em periódicos

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