Portal de Periódicos da CAPES

Artigo Acesso aberto Produção Nacional Revisado por pares

BIBTEX RIS

Human serum albumin-resveratrol complex formation: Effect of the phenolic chemical structure on the kinetic and thermodynamic parameters of the interactions

2019; Elsevier BV; Volume: 307; Linguagem: Inglês

10.1016/j.foodchem.2019.125514

1873-7072

Jaqueline de Paula Rezende, Eliara Acipreste Hudson, Hauster Maximiler Campos de Paula, Raíssa Soares Meinel, Adilson David da Silva, Luís Henrique Mendes da Silva, Ana Clarissa dos Santos Pires,

Analytical Chemistry and Chromatography

The thermodynamics and kinetics of binding between human serum albumin (HSA) and resveratrol (RES) or its analog (RESAn1) were investigated by surface plasmon resonance (SPR). The binding constant and the kinetic constants of association and dissociation indicated that RESAn1 has higher affinity toward HSA than does RES. The formation of these complexes was entropically driven ( [Formula: see text] , [Formula: see text] KJ mol-1). However, for both polyphenols, the activation energy (Eact) of association (a) of free molecules was higher than that for dissociation (d) of the stable complex ( [Formula: see text] KJ mol-1), and the rate of association was faster than that of dissociation since the activation Gibbs free energy (ΔG‡) was lower for the former (ΔGaHSA-RES‡≅54.73,ΔGdHSA-RES‡≅73.83,ΔGaHSA-RESAn1‡≅54.14,ΔGdHSA-RESAn1‡≅73.97 KJ mol-1). This study showed that small differences in the structure of polyphenols such as RES and RESAn1 influenced the thermodynamics and kinetics of the complex formation with HSA.