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The University of Southampton
Structural BiologyPart of Biological Sciences

Amyloid disease

The increasing prevalence of conditions such as Alzheimer’s, Parkinson’s and Huntington’s due to our ageing population represents a major challenge to society. Despite their diverse pathology, each of these diseases is characterised by the deposition of insoluble aggregates within the body, leading to the disruption of tissue and the functions they support.

NMR spectra of protein fibrils

These so called amyloid deposits arise through the miss-folding of proteins that are typically present in the body. The processes that initiate this transformation however, remain far from clear. The goal of our research is to understand the structural transitions that lead to the formation of these insoluble amyloid deposits and identify factors which promote its formation and/or stability. To address these challenges we are using a combination of liquid-state and solid-state NMR methods to map both the structural transitions associated with amyloid deposition and interactions with cellular factors which promote these processes.

Supervisor: Dr Phil Williamson

 



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