NR AUOU
AU Torrent,J.; Alvarez-Martinez,M.T.; Liautard,J.P.; Lange,R.
TI Modulation of prion protein structure by pressure and temperature
QU Biochimica et Biophysica Acta 2006 Mar; 1764(3): 546-51
PT journal article; review
AB 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.
ZR 42
MH Disulfides/*chemistry; Heat; Humans; Pressure; Prions/*chemistry; Protein Conformation; Protein Folding; Research Support, Non-U.S. Gov't; Temperature
AD INSERM U710, CC 105, IFR 122, Universite Montpellier 2, Place Eugene Bataillon, F-34095 Montpellier cedex 5, France. torrent@montp.inserm.fr
SP englisch
PO Niederlande