Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding

Eliara Acipreste Hudson; Hauster Maximiler Campos de Paula; Guilherme Max Dias Ferreira; Gabriel Max Dias Ferreira; Maria do Carmo Hespanhol; Luis Henrique Mendes da Silva; Ana Clarissa Dos S Pires

doi:10.1016/j.foodchem.2017.09.092

Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding

Food Chem. 2018 Mar 1:242:505-512. doi: 10.1016/j.foodchem.2017.09.092. Epub 2017 Sep 19.

Authors

Eliara Acipreste Hudson¹, Hauster Maximiler Campos de Paula², Guilherme Max Dias Ferreira³, Gabriel Max Dias Ferreira², Maria do Carmo Hespanhol², Luis Henrique Mendes da Silva⁴, Ana Clarissa Dos S Pires⁵

Affiliations

¹ Grupo de Termodinâmica Molecular Aplicada, Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa, Av, PH Rolfs, s/n, Campus Universitário, Viçosa, MG 36570-000, Brazil.
² Grupo de Química Verde Coloidal e Macromolecular, Departamento de Química, Universidade Federal de Viçosa, Av, PH Rolfs, s/n, Campus Universitário, Viçosa, MG 36570-000, Brazil.
³ Departamento de Química, Universidade Federal de Lavras, Caixa Postal 3037, Lavras, MG 37200-000, Brazil.
⁴ Grupo de Química Verde Coloidal e Macromolecular, Departamento de Química, Universidade Federal de Viçosa, Av, PH Rolfs, s/n, Campus Universitário, Viçosa, MG 36570-000, Brazil. Electronic address: luhen@ufv.br.
⁵ Grupo de Termodinâmica Molecular Aplicada, Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa, Av, PH Rolfs, s/n, Campus Universitário, Viçosa, MG 36570-000, Brazil. Electronic address: ana.pires@ufv.br.

PMID: 29037721
DOI: 10.1016/j.foodchem.2017.09.092

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 10⁵L·mol^-1 by fluorescence and microcalorimetric, and 10³ and 10⁴L·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=-8.67kJ·mol^-1), while microcalorimetry showed an entropic driven binding process (ΔH^○_cal=29.11kJ·mol^-1). For the unfolded BSA/curcumin complex, it was found thatp ΔH^○_F=-16.12kJ·mol^-1 and ΔH^○_cal=-42.63kJ·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.

Keywords: Analytical technique; BSA conformation; Curcumin; Curcumin (PubChem CID: 969516); Digitoxin (PubChem CID: 441207); Dimethyl sulfoxide (PubChem CID: 679); Ibuprofen (PubChem CID: 3672); Intermolecular interaction; Photodegradation; Warfarin (PubChem CID: 54678486).

MeSH terms

Animals
Calorimetry
Cattle
Curcumin / chemistry*
Entropy
Fluorescence
Kinetics
Molecular Conformation
Protein Binding
Serum Albumin, Bovine / chemistry*
Thermodynamics

Substances

Serum Albumin, Bovine
Curcumin