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AFM studies of beta-2 microglobulin amyloidosis

Reference	B16549
Principal Investigator / Supervisor	Professor Sheena Radford
Co-Investigators / Co-Supervisors	Professor David Smith, Dr Neil Thomson
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	184,448
Status	Completed
Type	Research Grant
Start date	02/09/2002
End date	02/09/2005
Duration	36 months

Abstract

Understanding the mechanism of amyloidosis, particularly under biologically relevant conditions, is a key challenge. Here we propose to address this issue by combining new developments in atomic force microscopy (AFM), including the use of carbon nanotubes as ultra-sharp probes, with the experimentally tractable, yet biologically important protein, beta2-microglobulin (beta2m). Specifically, we will use AFM to monitor the structure of fibrils formed in vitro and in vivo as well as the growth of individual fibrils in real time. In addition, we will perform novel studies of fibril growth on biologically relevant surfaces, and in this presence of amyloid-associated co-factors, to recreate the biological assembly process in vitro. Finally, we propose to use functionalised carbon nanotube tips to explore the feasibility of using chemical force microscopy to provide detailed structural information about large protein complexes such as these.

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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