Scientists at Cambridge’s Department of Chemistry have been able to construct a detailed map that shows how the formation of aberrant proteins in the brain can lead to a build-up so massive that it causes the development of numerous brain-damaging diseases, chief among them being Alzheimer’s.
In 2010, the Alzheimer’s Research Trust found that dementia alone cost the UK economy 23 billion euros, more than the costs of cancer and heart disease combined. Normally, proteins are made up of chemical building blocks known as amino acids, which are joined together in a code ordered by our DNA. New proteins appear as long, thin strips, which are then intricately folded to properly carry out their designated biological function. However, there are points at which the amyloid-beta protein misfolds or unfolds and gets tangled with other newly-made proteins. The tangles stick to one another until they number in the millions, known as amyloid fibrils, and they start the huge deposits of proteins known as plaque, which are so large, they become insoluble.
When the plaque in the brain reaches a critical level, a chain reaction is set off, and new focal points of tendrils form. From these tendrils, a smaller number of proteins, known as toxic oligomers, can easily diffuse through membranes, effectively killing neurons and causing memory loss as well as other dementia symptoms. This new groundbreaking information required scientists to come together, using kinetic experiments with a framework of theory. Master equations, more commonly used in the fields of chemistry and physics, aided researchers in their efforts to better understand Alzheimer’s, and how effectively to fight it.
University of Cambridge (2013, May 20). Molecular trigger for Alzheimer’s disease identified. ScienceDaily. Retrieved May 22, 2013,
Samuel I. A. Cohen, Sara Linse, Leila M. Luheshi, Erik Hellstrand, Duncan A. White, Luke Rajah, Daniel E. Otzen, Michele Vendruscolo, Christopher M. Dobson, and Tuomas P. J. Knowles. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences, 2013; DOI: 10.1073/pnas.1218402110
By Lauren Horne
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