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

Jaqueline de Paula Rezende; Eliara Acipreste Hudson; Hauster Maximiler Campos De Paula; Raissa Soares Meinel; Adilson David Da Silva; Luis Henrique Mendes Da Silva; Ana Clarissa Dos Santos Pires

doi:10.1016/j.foodchem.2019.125514

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

Food Chem. 2020 Mar 1:307:125514. doi: 10.1016/j.foodchem.2019.125514. Epub 2019 Oct 1.

Authors

Jaqueline de Paula Rezende¹, Eliara Acipreste Hudson¹, Hauster Maximiler Campos De Paula², Raissa Soares Meinel³, Adilson David Da Silva³, Luis Henrique Mendes Da Silva⁴, Ana Clarissa Dos Santos Pires⁵

Affiliations

¹ Applied Molecular Thermodynamics Group (THERMA), Department of Food Technology, Federal University of Viçosa, Av. P. H. Rolfs s/n, 36570900 Viçosa, MG, Brazil.
² Colloidal and Macromolecular Green Chemistry Group (QUIVECOM), Department of Chemistry, Federal University of Viçosa, Av. P. H. Rolfs s/n, 36570900 Viçosa, MG, Brazil.
³ Department of Chemistry, Institute of Exact Sciences (I.C.E.), Federal University of Juiz de Fora, 36036-900 Juiz de Fora, MG, Brazil.
⁴ Colloidal and Macromolecular Green Chemistry Group (QUIVECOM), Department of Chemistry, Federal University of Viçosa, Av. P. H. Rolfs s/n, 36570900 Viçosa, MG, Brazil. Electronic address: luhen@ufv.br.
⁵ Applied Molecular Thermodynamics Group (THERMA), Department of Food Technology, Federal University of Viçosa, Av. P. H. Rolfs s/n, 36570900 Viçosa, MG, Brazil. Electronic address: ana.pires@ufv.br.

PMID: 31639576
DOI: 10.1016/j.foodchem.2019.125514

Abstract

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 (E_act) 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 (ΔG_aHSA-RES^‡≅54.73,ΔG_dHSA-RES^‡≅73.83,ΔG_aHSA-RESAn1^‡≅54.14,ΔG_dHSA-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.

Keywords: Activated complex; Comparative study; Human serum albumin; Human serum albumin (PubChem CID: 72941834); Kinetic constants; Resveratrol; Resveratrol (PubChem CID: 445154); Resveratrol analogue; Thermodynamic binding.

MeSH terms

Humans
Hydrogen-Ion Concentration
Immobilized Proteins / chemistry
Immobilized Proteins / metabolism
Kinetics
Phenols / chemistry*
Protein Binding
Resveratrol / chemistry
Resveratrol / metabolism*
Serum Albumin, Human / chemistry
Serum Albumin, Human / metabolism*
Surface Plasmon Resonance
Temperature
Thermodynamics

Substances

Immobilized Proteins
Phenols
Resveratrol
Serum Albumin, Human