Anybody who has cooked an egg will know that as soon as you apply some heat, the egg starts to harden. The more heat you apply and the longer you apply it for, the harder the egg gets. This is thanks to the protein in the eggs unfolding as heat is applied, forming new bonds, clumping together (aggregating) and hardening. While that might be a good outcome for your breakfast, what happens inside our own bodies when proteins are stressed? Scientists at the University of Zululand are asking just this question.
Professor Addmore Shonhai explains that in our own bodies, when proteins are subjected to heat stress they tend to misfold and aggregate, leading to possible cellular toxicity. It also means that the protein is no longer functional. That is worrying considering the crucial role proteins, like enzymes, play in our bodies.
Hsp70, one of the so-called heat shock proteins (hsp) (also known as a molecular chaperone) is fairly well characterized in the literature for its role naturally in preventing protein misfolding after heat stress. New research suggests that capped gold nanomaterials may also come to the rescue.
A study conducted by Sfiso Luthuli, an Msc student in Prof. Addmore Shonhai’s lab based at the University of Zululand has shown that cysteine-capped gold nanoparticles protected proteins from heat-induced stress in vitro.
It appears that the key mechanism at play is that the capped nanoparticles suppresses the heat-induced aggregation of proteins, therefore acting like an artificial chaperone.
The work has bigger implications for understanding how gold nanoparticles interact with proteins, particularly for research in drug delivery using these nanomaterials.
The research, published in IUBMB Life also suggested that the gold nanoparticles augmented the function of Hsp70 proteins.
In future studies, Prof. Shonhai, in collaboration with Prof. Neerish Revaparasadu, (who holds a SARChI Chair in Nanotechnology at UZ) aims to understand more clearly the precise mechanism involved in this newer role for gold nanoparticles.
Link to the published paper: http://onlinelibrary.wiley.com/doi/10.1002/iub.1146/abstract
Writer: Janice Limson