The formation of protein gel networks in aqueous systems is a result of protein intermolecular interactions after an energy input, like heating. In this research, we report that a redox reaction between Au3+ions and proteins can also lead to the formation of a protein gel network. Amino acids, like cysteine and tyrosine, get oxidized and form covalent bonds with neighboring protein molecules, while Au3+ions get reduced to Au+and Au0, nucleate and form gold nanoparticles. The protein gel network formation occurs within 2 h at room temperature and can be tuned by varying Au3+/protein ratio and accelerated by increasing the incubation temperature. The proposed Au3+-induced gel network formation was applied to different proteins, like egg yolk high-density lipoprotein, bovine serum albumin and whey protein. This research opens new insights for the investigation of the metal-protein interactions and may aid in the design of novel hybrid-soft nanocomposite materials.
CITATION STYLE
Schijven, L. M. I., Saggiomo, V., Velders, A. H., Bitter, J. H., & Nikiforidis, C. V. (2021). Au3+-Induced gel network formation of proteins. Soft Matter, 17(42), 9682–9688. https://doi.org/10.1039/d1sm01031j
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