Misfolding of the prion protein: linking biophysical and biological approachesSylvie Noinville, Jean-François Chich and Human Rezaei
Institut National de la Recherche Agronomique, Virologie et Immunologie Moléculaires, F-78352 Jouy-en-Josas, France
Received 23 November 2007; accepted 03 June 2008; published online 05 June 2008
Abstract - Prion diseases are a group of neurodegenerative diseases that can arise spontaneously, be inherited, or acquired by infection in mammals. The propensity of the prion protein to adopt different structures is a clue to its pathological and perhaps biological role too. While the normal monomeric PrP is well characterized, the misfolded conformations responsible for neurodegeneration remain elusive despite progress in this field. Both structural dynamics and physico-chemical approaches are thus fundamental for a better knowledge of the molecular basis of this pathology. Indeed, multiple misfolding pathways combined with extensive posttranslational modifications of PrP and probable interaction(s) with cofactors call for a combination of approaches. In this review, we outline the current physico-chemical knowledge explaining the conformational diversities of PrP in relation with postulated or putative cellular partners such as proteic or non-proteic ligands.
Key words: structure / membrane / oligomer / kinetics
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© INRA, EDP Sciences 2008