Probing the interaction between encapsulated ethoxyquin and its β-cyclodextrin inclusion complex with bovine serum albumin

Abstract

Ethoxyquin (EQ) is a synthetic antioxidant that is derived from quinolines and found in many meat products. EQ is strictly regulated in feed due to its potential health implications. An investigation of the interaction mechanism between EQ and transporter protein before and after β-cyclodextrin (β-CD) encapsulation was conducted with the use of multi-spectroscopy, cyclic voltammetry, and molecular docking. EQ formed complexes with bovine serum albumin (BSA), and affected secondary structure and microenvironment polarity of BSA. However, at 298 K, EQ's fluorescence quenching constants decreased from (9.81 ± 0.05) × 103 L mol−1 to (4.94 ± 0.09) × 103 L mol−1, binding constants decreased from (10.28 ± 0.02) × 103 L mol−1 to (2.08 ± 0.07) × 103 L mol−1, after encapsulation in β-CD as well as the binding distance increased. β-CD contains part of EQ in its hydrophobic cavity, inhibiting its binding to BSA. β-CD inclusion complex prevented adverse effects of EQ on BSA conformation. However, β-CD encapsulation had no effect on EQ's antioxidant activity.