Issue 42, 2021

Au3+-Induced gel network formation of proteins

Abstract

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.

Graphical abstract: Au3+-Induced gel network formation of proteins

Supplementary files

Article information

Article type
Paper
Submitted
14 Jul 2021
Accepted
04 Oct 2021
First published
11 Oct 2021
This article is Open Access
Creative Commons BY-NC license

Soft Matter, 2021,17, 9682-9688

Au3+-Induced gel network formation of proteins

L. M. I. Schijven, V. Saggiomo, A. H. Velders, J. H. Bitter and C. V. Nikiforidis, Soft Matter, 2021, 17, 9682 DOI: 10.1039/D1SM01031J

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements