A novel approach to unravelling the mysteries of Alzheimer’s
Posted: 16 December 2019 | Dr Sean Devenish (Fluidic Analytics), Professor Tuomas Knowles (University of Cambridge) | No comments yet
The heterogenous and dynamic nature of protein aggregates makes them a particularly challenging class of structures to study. In this article, Professor Tuomas Knowles and Dr Sean Devenish present a novel approach to studying protein structures that could aid in understanding the complexities of Alzheimer’s disease and identify future therapeutic targets.
THE MOLECULAR machinery of living cells is largely built from protein molecules. These components interact to form complexes that drive most cellular functions. In many cases, proteins find their correct partners and self-assemble into their intended structures without difficulty. In rare cases, however, proteins may bind to an incorrect partner, or to the correct partner but in an incorrect manner, resulting in the formation of aberrant complexes, which are, in most cases, associated with disease. One of the most dramatic manifestations of this type of protein misassembly is the formation of amyloid aggregates in Alzheimer’s disease. With nearly 10 million new cases every year – one every three seconds – dementia is already a public health priority and with cases set to triple and reach 152 million by 2050,1 new experimental methods to understand the aberrant molecular structures formed in diseases such as Alzheimer’s are critical to develop new drugs.