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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Experimental Approaches to Tse Prevention Via Inhibition of Prion Formation

Author(s): Galatia Politopoulou

Volume 11, Issue 3, 2004

Page: [249 - 255] Pages: 7

DOI: 10.2174/0929866043407192

Price: $65

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


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