title: Modulation of prion protein structure by pressure and temperature.
abstract: High pressure and temperature have been used efficiently to shed light on prion protein structure and folding. These physical parameters induce different conformational states of the prion protein, suggesting that prion structural changes occur within a complex energy landscape. Pressure has been used to prevent and even reverse prion protein aggregation. Alternatively, depending on experimental conditions, pressure also promotes prion protein aggregation leading to the formation of amorphous aggregates and amyloid fibrils. The latter ones show all characteristics of the pathogenic scrapie form. Furthermore, the pressure effects on prion protein structure appear to be strongly dependent on the integrity of the disulfide bond. In this paper, we discuss the mechanism and the origin of these opposing effects of pressure, taking the truncated form of hamster prion protein (SHaPrP(90-231)) as a model.
authors.affiliation: INSERM U710, CC 105, IFR 122, Université Montpellier 2, Place Eugène Bataillon, F-34095 Montpellier cédex 5, France. torrent@montp.inserm.fr
authors.forename: Joan
authors.initials: J
authors.lastname: Torrent
authors.forename: Maria Teresa
authors.initials: MT
authors.lastname: Alvarez-Martinez
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Liautard
authors.forename: Reinhard
authors.initials: R
authors.lastname: Lange
mesh_terms: D004220:Disulfides / Q000737:chemistry*; D006358:Hot Temperature; D006801:Humans; D011312:Pressure; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013696:Temperature
chemical_list: D004220:Disulfides; D011328:Prions