This multidisciplinary project involving expertise from both Chemical & Process Engineering and Physics Departments at the University of Stathclyde aims to understand how and why amyloid fibril structures nucleate and grow. The project combines theory and simulations, as well as experimental probes of controlled samples.
Beta-amyloid is a protein associated with Alzheimer’s disease, some forms of Lewy body dementia, and many more diseases. It is a widely accepted theory that these proteins misfold and start to aggregate, disrupting cell membranes. The degeneration of brain cells then leads to the development of the amyloidosis disease. However, questions remain about the mechanisms behind this misfolding/aggregation process due to the limitations of experimental techniques. This is where molecular modelling and simulations could enable a deeper understanding of the process.
Preliminary data obtained from Monte Carlo and Molecular Dynamic simulations have shown novel insight into how the fibrils grow which is complemented by an emerging theoretical framework. The present aim of the project is to robustly develop these new ideas via Molecular Dynamics and Monte Carlo Simulations and to supplement these theoretical models with experimental data. Ultimately we wish to understand how we may halt the aggregation pathways of the protein associated with the amyloidosis disease progression.
For more information about the project contact Dr Paul Mulheran (firstname.lastname@example.org), Senior Lecturer at the Department of Chemical and Process Engineering at the University of Strathclyde or Dr Olaf Rolinski (email@example.com), Senior Lecturer at the Department of Physics at the University of Strathclyde.
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