What do Alzheimers and body armour have in common? The answer could lie in the structures formed when proteins self-assemble at the nanoscale.
At the end of last year, The Daily Telegraph Science Editor Roger Highfield wrote in an article:
“The protein linked with Alzheimer’s disease has inspired the design of “nanoyarns” that could be put to a vast range of uses, from body armour to parachutes and super strong nets.”
The research, published in the journal Science by Tuomas Knowles and other members of Mark Welland’s team at the University of Cambridge (U.K.), studied the properties of nanometre-diameter fibrils formed from misfolding proteins. In tests, these fibrils showed the potential to outperform many conventional natural materials, leading to Knowles and colleagues referring to them as “a class of high performance biomaterials”.
But what caught my attention was that the researchers were using amyloid proteins—a class of proteins associated with diseases that include Alzheimers, Parkinsons and type II diabetes. Common to all amyloid diseases are proteins that misfold, and end up forming long, thin, insoluble fibrils that accumulate in the body—the same fibrils that the Cambridge team saw as a potential new nanoscale biomaterial.
Fibrillation—the formation of fibrils through misfolding and self-assembly—occurs because of physical and chemical changes at the nanoscale. And this raises the possibility of modifying the process by introducing nanometre-scale materials to the protein environment. Nanoparticles might be able to prevent or treat amyloid diseases by preventing fibrillation (an active area of research), but they might also exacerbate the process.
In a ground-breaking study, Sarah Linse and colleagues demonstrated last year that—under certain circumstances—nanoparticles can increase the rate of fibrillation in amyloid proteins. In other words, nanoparticles can change the way some proteins behave.
This research was far removed from predicting possible health impacts of nanoparticles in people—the proteins were in a cell free environment that was adjusted to encourage fibrillation. Nevertheless, it was an important step towards understanding how nanomaterials and biomolecules can interact at the nanoscale, with unexpected consequences.
Both of these studies serve to highlight the multi-faceted nature of nanotechnology. Nanotech is gloriously messy: in this one example, it could conceivably hold the key to both the cause and the cure of a disease, as well as the basis for a spin-off technology! This “messiness” makes nanotechnology an incredibly exciting and innovating field, liberating scientists and thinkers to cross boundaries and explore new ideas and possibilities. Granted, it muddies the debate over how to develop safe nanotechnologies, and it forces us to make decisions on the best possible science rather than speculation (which is why we so desperately need better risk research strategies).
But at the end of the day, it is this mixing-up of expertise and ideas that will stimulate truly innovative developments that not only lead to new applications, but point the way to using them as safely as possible.
How else could you achieve a fusion of ideas that links nanoparticles to protein misfolding, and protein misfolding to nanomaterials?
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This post first appeared on the SAFENANO blog in January 2008