Dynamics of amyloid protein fibril elongation using isotope-labelled SANS

DOI

This proposal combines small-angle neutron scattering with novel labelling strategies to investigate “amyloid” protein fibrils. Variations in packing and in the dynamics of elongation and breakage underpin phenomena ranging from non-genetic heredity in yeast, to diseases such as Alzheimer’s, BSE and CJD. Most solution methods to monitor growth dynamics only give information on the overall % of material transformed from non-fibrillar to fibrillar forms. They cannot determine length distribution or linear growth rates, but instead convolute the two; in other words, they cannot distinguish a few long fibrils each growing quickly, from many short fibrils each growing more slowly. We will determine both fibril lengths and linear growth rates using a novel SANS approach with labelled ends growing on contrast-matched "seed" fibrils

Identifier
DOI https://doi.org/10.5286/ISIS.E.92922164
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/92922164
Provenance
Creator Dr Trevor Forsyth; Mr Ben Eves; Dr Ann Terry; Dr James Doutch; Dr Adam Squires; Dr Michael Haertlein
Publisher ISIS Neutron and Muon Source
Publication Year 2021
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2018-05-14T08:00:00Z
Temporal Coverage End 2018-05-18T08:00:10Z