Award details

Design folding and co-operative interactions in beta-sheet peptides

ReferenceB13465
Principal Investigator / Supervisor Professor Mark Searle
Co-Investigators /
Co-Supervisors
Institution University of Nottingham
DepartmentSch of Chemistry
Funding typeResearch
Value (£) 167,596
StatusCompleted
TypeResearch Grant
Start date 01/10/2000
End date 07/01/2004
Duration39 months

Abstract

The importance of a beta-sheet structure in the formation of amyloid fibrils, and their role in a variety of pathological disease states (Alzheimers and BSE) suggests that model beta-sheet peptides may provide insight into the molecular basis and sequence dependence of sheet formation, the origin of their stability and the importance of co-operative interactions in their propagation. We investigate these phenomena using rationally designed two and three-stranded beta-sheet peptides using a variety of spectroscopic probes and theoretical methods to simulate folding. We focus on a quantitative description of stability and co-operative interactions both parallel and perpendicular to the strand direction using model systems already established in our group, and expand the design strategy to incorporate arrays of ionic interactions in addition to conventional hydrophobic motifs.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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