4.6 Article

Interaction mechanism between ZnO nanoparticles-whey protein and its effect on toxicity in GES-1 cells

Journal

JOURNAL OF FOOD SCIENCE
Volume 87, Issue 6, Pages 2417-2426

Publisher

WILEY
DOI: 10.1111/1750-3841.16193

Keywords

cytotoxicity; interaction; mechanism; whey protein; zinc oxide nanoparticles

Funding

  1. Guangdong Province Key Field R&D Program Project [2019B020210002]

Ask authors/readers for more resources

This study focused on the interaction between zinc oxide nanoparticles (ZnO NPs) and whey protein (WP). The results indicated that ZnO NPs had an inhibitory effect on cell activity, but this effect could be reduced when added at a concentration of 50 μg/ml. The interaction between ZnO NPs and WP involved both dynamic and static quenching. The binding sites between ZnO NPs and WP were considered to be hydrogen bonding and van der Waals forces. The interaction resulted in structural changes in WP and the exposure of hydrophobic groups, thereby reducing the hydrophobicity of the microenvironment. This study provides a theoretical basis for understanding the interaction between food ingredients and nanomaterials, evaluating nanomaterial toxicity, and exploring nanomaterial applications in the food industry.
The interaction between zinc oxide nanoparticles (ZnO NPs) and whey protein (WP) was studied. The gastric epithelial cell line (GES-1) was used to evaluate the toxicity intensity of ZnO NPs. The interaction mechanism of ZnO NPs and WP was studied by spectroscopic techniques. The results showed that the inhibitory effect of ZnO NPs on cells activity could be reduced when added to ZnO NPs at a concentration of 50 mu g/ml. The fluorescence quenching mechanism of ZnO NPs on WP is a combination of dynamic and static quenching. The interaction force between ZnO NPs and WP can be considered as H-bond and VdW force, and they have two binding sites. The interaction between WP and ZnO NPs leads to the loosening of the structural skeleton of WP and the extension of peptide chain, which exposes the tyrosine (Tyr) and tryptophan (Trp) hydrophobic groups in the hydrophobic region of protein molecules and reduces the hydrophobicity of the microenvironment. The ZnO NPs might form a complex with WP through H-bond, hydrophobic interactions, and so on, leading to peptide chain rearrangement, and finally causing changes in the secondary structure of alpha-helix. This study provides a theoretical basis for future research on the interaction between food ingredients and nanomaterials, the evaluation of toxicity of nanomaterials and the application scope of nanomaterials in food field. Practical Application

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available