Experimental Approaches to Tse Prevention Via Inhibition of Prion Formation

Author: Politopoulou G.

Source: Protein and Peptide Letters, Volume 11, Number 3, June 2004 , pp. 249-255(7)

Publisher: Bentham Science Publishers

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Abstract:

Transmissible spongiform encepahalopathies (TSEs) are fatal diseases that damage the central nervous system. TSEs are unique in that they may be inherited, infectious or spontaneous. The central pathogenic agent is thought to be a conformationally distinct form (PrPSc) of the endogenous prion protein(PrPc), which is high in beta-sheet content and is resistant to proteases; infectivity is thought to involve formation of PrPSc via imprinting of abnormal conformation on the normal form of the protein (PrPc) by seeds of PrPSc. A number of compounds found to inhibit the conversion of PrPc to PrPSc have been proposed as therapeutics to halt TSEs.

Keywords: spongiform encephalopathies; prions; beta-sheet; proline peptides

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866043407192

Affiliations: 1: Department of Rheumatology, Avon Orthopaedic Centre, Southmead Hospital, University of Bristol, Bristol BS10 5NB.

Publication date: 2004-06-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.