Use este identificador para citar ou linkar para este item:
https://locus.ufv.br//handle/123456789/18774
Tipo: | Artigo |
Título: | Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding |
Autor(es): | 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. |
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. |
Palavras-chave: | Curcumin Intermolecular interaction Analytical technique BSA conformation Photodegradation |
Editor: | Food Chemistry |
Tipo de Acesso: | Elsevier Ltd |
URI: | https://doi.org/10.1016/j.foodchem.2017.09.092 http://www.locus.ufv.br/handle/123456789/18774 |
Data do documento: | 18-Set-2017 |
Aparece nas coleções: | Artigos |
Arquivos associados a este item:
Arquivo | Descrição | Tamanho | Formato | |
---|---|---|---|---|
artigo.pdf Until 2100-12-31 | Texto completo | 670,51 kB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
Os itens no repositório estão protegidos por copyright, com todos os direitos reservados, salvo quando é indicado o contrário.