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Probing human lysozyme amyloid formation and inhibition using camel antibody fragments

Reference	B16927
Principal Investigator / Supervisor	Professor Carol Robinson
Co-Investigators / Co-Supervisors	Professor David Archer, Professor Sir Christopher Dobson, Dr Mireille Dumoulin
Institution	University of Cambridge
Department	Chemistry
Funding type	Research
Value (£)	384,528
Status	Completed
Type	Research Grant
Start date	01/01/2002
End date	31/12/2004
Duration	36 months

Abstract

Camelid antibodies to wild-type human lysozyme will be produced such that they cross-react with single amino acid variants associated with amyloid disease. We will examine a range of camelid antibodies produced by phage display to investigate the effects of their binding on the conformational stability of the variant proteins. Using these antibodies as structural probes we shall investigate the nature of the structural and dynamical perturbations induced by mutations and their relationship to amyloidogenicity. In addition to defining in greater detail the mechanism of the conversion of proteins into amyloid fibrils we shall investigate the possibility of the use of antibodies to inhibit aggregation to promote the dissolution of fibrils.

Summary

unavailable

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

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