Probing gold nanoparticles for the desensitization to β-lactoglobulin from binding mechanism, structure and IgE binding changes.

Because of the adsorption of proteins, gold nanoparticles (AuNPs) create potential biological risks in biomedicine, leading to the formation of the protein corona. This adsorption is mainly due to the formation of gold-sulfur (AuS) covalent bonds between the AuNPs and the -SH groups, causing bioactivity denaturation and biological problems; however, it could also lead to some biological benefits. We explored AuNPs as a potential material for desensitization to allergens, such as β-lactoglobulin (βLG). To address the desensitization of AuNPs, we investigated the binding mechanism and the specific relationship of the time evolution of AuS bond, secondary structure, and allergy changes. The formation of AuS bond takes approximately 9 h, consistent with the complete changes time in secondary structure and immunoglobulin E (IgE) combining capacity of the βLG, decreasing allergic reactions. These results indicate that AuNPs have the potential to minimize allergic reactions in the future.