Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/33889
Título : Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding
Autor: 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.
Palavras-chave: Curcumin
Intermolecular interaction
Analytical technique
Bovine serum albumin (BSA)
Photodegradation
Publicador: Elsevier
Data da publicação: Mar-2018
Referência: 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.
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.
URI: https://www.sciencedirect.com/science/article/pii/S0308814617315674?via%3Dihub
http://repositorio.ufla.br/jspui/handle/1/33889
Idioma: en_US
Aparece nas coleções:DQI - Artigos publicados em periódicos

Arquivos associados a este item:
Não existem arquivos associados a este item.


Os itens no repositório estão protegidos por copyright, com todos os direitos reservados, salvo quando é indicado o contrário.