Experimental approaches to TSE prevention via inhibition of prion formation

被引：1

作者：

Politopoulou, G ^{[1
]}

机构：

[1] Univ Bristol, Southmead Hosp, Avon Orthopaed Ctr, Dept Rheumatol, Bristol BS10 5NB, Avon, England

来源：

PROTEIN AND PEPTIDE LETTERS | 2004年 / 11卷 / 03期

关键词：

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

D O I：

10.2174/0929866043407192

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：249 / 255

页数：7

共 38 条

[1] Characterization and polyanion-binding properties ef purified recombinant recombinant protein [J].