Molecular docking studies and physicochemical properties on the interaction of xanthone with whey protein (β-lactoglobulin and α-lactalbumin)

Abstract

Whey protein (WP) is a good encapsulating material of food applications and can act as a delivery vehicle for bioactive compounds, including xanthone. The objective of this research is to analyze the interaction of WP with xanthone using molecular modeling and investigate the effect of whey protein at different concentration of xanthone (0.025%; 0.05% and 0.1% (v/v) ) on emulsion stability, antioxidant, and chemical structure by FTIR (Fourier Transform Infrared). Each treatment was replicated four times. The docking studies were performed with Programme Autodock Vina PyRx 0.8. Molecular docking studies revealed that interaction of xanthone and whey protein are stabilized by hydrogen bonds, hydrophobic interaction, and van der walls bond. The different concentrations of xanthone gave a highly significant effect on emulsion stability and didn’t give a significant difference between the three treatments on antioxidant activity. FTIR result showed that wave numbers 690-900 and 3010-3100 cm-1 indicate the presence of CH groups and 1500-1600 cm-1 which may indicate the presence of C = C aromatic ring groups, respectively. The highest emulsion stability was at 0.1% with 99.23%. The highest antioxidant was at 0.1% with 86.40%.

Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks

“…Site II is located on the outer surface of β-LG, and the main residues are Trp19, Tyr20, Tyr42, Gln44, Gln59, Gln68, Leu156, Glu157, Glu158 and His161 [ 11 ]. LUT bound with Thr18, Val43, and Leu156 through a hydrogen bond, which was in agreement with the results reported by Rahayu et al [ 32 ]. Eight amino acid residues of β-LG (Trp19, Ser21, Tyr42, Glu45, Gln59, Glu158, Gln159 and His161) interacted with LUT through van der Waals bonds.…”

A review of polyphenol and whey protein-based conjugates

“…Whey proteins have numerous charged groups, hydrogen receptors, and non-polar groups on their surface, which makes them available for hydrophobic interactions, electrostatic interactions, and hydrogen bonding (Bartolomé et al 2000;Buitimea et al 2016;Khalifa et al 2018). Whey protein fibril complexes with carvacrol improves the film-forming ability, emulsifying ability, and their antimicrobial activity; WP complex formation with xanthone enhances the protein emulsifying property compared to WPs alone (Rahayu et al 2020;Wang et al 2020a,b). The emulsion stability was improved because of the reduction in hydrophobic attraction and increased electrostatic and steric repulsion between the protein-coated oil drops.…”