Surface plasmon resonance study of interaction between lactoferrin and naringin

Natália M Nunes; Hauster M C de Paula; Yara L Coelho; Luis Henrique M da Silva; Ana Clarissa S Pires

doi:10.1016/j.foodchem.2019.125022

Surface plasmon resonance study of interaction between lactoferrin and naringin

Food Chem. 2019 Nov 1:297:125022. doi: 10.1016/j.foodchem.2019.125022. Epub 2019 Jun 15.

Authors

Natália M Nunes¹, Hauster M C de Paula², Yara L Coelho², Luis Henrique M da Silva³, Ana Clarissa S Pires⁴

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 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.
⁴ 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: 31253281
DOI: 10.1016/j.foodchem.2019.125022

Abstract

Lactoferrin (LF) is a glycoprotein that serves as a potential vehicle for small bioactive molecules in food. In an effort to improve this functionality, the kinetic and thermodynamic interaction of LF with naringin (NR) was studied by surface plasmon resonance (SPR). The results demonstrated that the association rate constant between LF and NR was 5.00 × 10⁴ M^-1 s^-1, while the dissociation rate of the complex was 0.36 s^-1, at 25 °C. The stable complex predominated over free molecules (ΔG_25°C⁰=-29.35 kJ mol^-1), and the binding constant was 1.39 × 10⁵ M^-1, at 25 °C. The association of LF and NR to form an intermediate complex occurred in multi-steps. Nevertheless, the intermediate complex formation from the dissociation of the stable complex occurred in a single step with the activation energy independent of temperature. This study provides an important basis to explore LF as a vehicle for bioactive molecules.

Keywords: Bovine lactoferrin; Bovine lactoferrin (PubChem CID: 126456119); Flavonoid; Kinetic binding; Naringin (PubChem CID: 442428); SPR; Thermodynamic binding.

MeSH terms

Animals
Cattle
Flavanones / chemistry*
Flavanones / metabolism
Kinetics
Lactoferrin / chemistry*
Lactoferrin / metabolism
Protein Binding
Surface Plasmon Resonance*
Temperature
Thermodynamics

Substances

Flavanones
Lactoferrin
naringin