A new mathematical framework for AB peptide assembly in Alzheimer's disease
Lead Research Organisation:
University of Sheffield
Department Name: Molecular Biology and Biotechnology
Abstract
Protein misfolding is responsible for some of the most prevalent aging diseases. Fibrillar "amyloid" species accumulate as extracellular plaques or intracellular tangles and act as sinks for neurotoxic soluble species. Our data show that current models of protein polymerisation are inapplicable to amyloids such as AB. This is because historical models were developed for proteins with a narrow range of folds, while amyloids have complex folding landscapes and a vast array of conformations.
Our proposal is to use techniques that will remove bias in our search for mechanisms, producing emergent behaviours from simulation rather than simply confirming or negating existing theories. This represents a step-change in our approach to amyloid formation. To date, theoreticians have not taken full advantage of structural and kinetic data. The novelty of this proposal is its "multi-scale" nature and the combination of top-down and bottom up approaches
Our proposal is to use techniques that will remove bias in our search for mechanisms, producing emergent behaviours from simulation rather than simply confirming or negating existing theories. This represents a step-change in our approach to amyloid formation. To date, theoreticians have not taken full advantage of structural and kinetic data. The novelty of this proposal is its "multi-scale" nature and the combination of top-down and bottom up approaches
Organisations
People |
ORCID iD |
Rosemary Ann Staniforth (Primary Supervisor) |
Studentship Projects
Project Reference | Relationship | Related To | Start | End | Student Name |
---|---|---|---|---|---|
BB/M011151/1 | 30/09/2015 | 29/09/2023 | |||
2109094 | Studentship | BB/M011151/1 | 30/09/2018 | 29/09/2022 |