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Carbohydrate-mediated interactions of PrPc

Reference	BBS/E/I/00000646
Principal Investigator / Supervisor	Dr James Hope
Co-Investigators / Co-Supervisors
Institution	The Pirbright Institute
Department	The Pirbright Institute Department
Funding type	Research
Value (£)	19,873
Status	Completed
Type	Institute Project
Start date	02/10/1997
End date	01/10/2000
Duration	36 months

Abstract

Cellular prion protein (PrPC) binds to acidic polysaccharides and these interactions can inhibit the accumulation of its disease-specific isoform, PrPSc, during the development of scrapie, BSE and other transmissible spongiform encephalopathies. No sequences of natural saccharide ligands for PrPC are known and we are using soluble, recombinant PrP (recPrP) several denatured and re- folded from E. Coli inclusion bodies several to screen libraries of lipid-linked oligosaccharides from N- and O- glycosylated glycoproteins, proteoglycans and glycolipids purified from mouse and hamster brain. State-of-the-art analytical and ligand discovery techniques are being applied to enable the sensitive detection of oligosaccharide ligands and their structural characterisation. These natural PrP- binding molecules will provide lead structures for the development of more specific inhibitors of PrPC to PrPSc conversion.

Summary

unavailable

Committee	Closed Committee - Agri-food (AF)
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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