NR ATRJ
AU Torrent,J.; Alvarez-Martinez,M.T.; Balny,C.; Liautard,J.P.; Lange,R.
TI Insights into prion protein misfolding events from high pressure studies
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Structure of PrP and molecular determinants of infectivity STRCT-25
PT Konferenz-Poster
AB
High pressure (up to 600 MPa) provides a convenient means to populate and characterize partially unfolded states of the prion protein. Depending on the experimental conditions, such species aggregate into thick dense networks of amyloid fibrils, which coexist with amorphous aggregates.
In contrast to such aggregation-prone effect, pressures of 200 MPa prevent the formation of temperature-induced amorphous aggregates, thus enabling the analysis of the heat-induced unfolding pathway of PrP leading to a soluble unfolded state. Such relatively low pressure also solubilizes and correctly refolds PrP aggregates initially formed at high temperature.
The observed opposing pressure effects leading to different PrP structural states depend on the precise physical-chemical conditions, and reveal that these states may be differentiated by their total molecular volume. This suggests that the PrPc to PrPsc transconformation is a rather unusual mechanism, involving alternative paths on a complex energy landscape.
AD J.Torrent, C.Balny, R.Lange, INSERM U710, Université Montpellier 2, France.; M.T.Alvarez-Martinez, J.P.Liautard, INSERM U431, Université Montpellier 2, France
SP englisch
PO Deutschland