NR AWPG
AU Tsiroulnikov,K.; Muronetz,V.; Chobert,J.M.; Haertle,T.
TI Rapid aggregation of recombinant ovine prion protein induced by submicellar concentrations of phospholipids
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions S-26
PT Konferenz-Poster
AB Transformation of prion protein (PrP) in its insoluble amyloid form provokes neurodegenerative disorders - transmissible spongiform encephalopathies. PrP is connected to neuron membrane by covalently linked glycosylphosphatidylinositol (GPI) anchor. Previous studies described structural alterations and formation of aggregated structures of PrP bound to lipid membranes. Current study demonstrates that PrPrec may interact with individual phosphatidylinositol and phosphatidylethanolamine molecules non-included into membrane structures, and these interactions induce rapid aggregation of PrP protein, which takes place even in presence of very low concentrations of lipid. Lipid micelles prevent formation of large PrP aggregates and provoke increase in ß-sheet structure of protein. Thus, liberation of PrP from membrane and direct interaction with its own GPI moiety, as well as with membrane lipids, can increase risk of the formation of amyloid structures. The authors acknowledge the support from GIS Prion, the European REX Neuroprion Taskgroup PRIONINACT Dec-1 (Decontamination) and INTAS project # 03-51-4813.
AD K. Tsiroulnikov: Institut National de la Recherche Agronomique, BIA-FIPL, B.P. 71627, F-44316 Nantes Cedex 3, France; Laboratory of Proteolytic Enzyme Chemistry, Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry of RAS, Moscow, Russia; J.-M. Chobert, T. Haertlé: Institut National de la Recherche Agronomique, BIA-FIPL, B.P. 71627, F-44316 Nantes Cedex 3, France; V. Muronetz: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie gory, Moscow 119992, Russia
SP englisch
PO Italien