Characterisation of toxic oligomer present in Alzheimer’s disease-associated amyloid fibrillation proces
Research area: Computational Structural Biology
Associate members: Andrea Cavalli
Status: In progress
Alzheimer’s disease (AD) is recognized as the most spread neurodegenerative disease affecting over 30 million people worldwide. The development of the disorder has been linked to the presence of extracellular beta-amyloid (Ab) peptide aggregates of different sizes. Ab oligomeric species formed at early stages of the aggregation process are leading candicates for causing AD. Thus, targeting oligomers can be a very valuable strategy to combat Alzheimer’s disease. However, the molecular mechanism underlying the self-assembly of the different Ab species is not fully understood and it is not clear how the early soluble oligomeric species associate to form protofibrils and, subsequently, mature fibrils.
The main objective of this project is to apply computational techniques to elucidate small angle X-ray scattering (SAXS) data collected by our collaborators at University of Cambridge (Prof. M. Vendruscolo group) and resolve major coexisting components in Ab fibrillation process.