Reference : Interaction of the 106-126 prion peptide with lipid membranes and potential implicati...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63493
Interaction of the 106-126 prion peptide with lipid membranes and potential implication for neurotoxicity.
English
Dupiereux-Fettweis, Ingrid mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine >]
Zorzi, Willy mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine - Département des sciences biomédicales et précliniques >]
Lins, Laurence mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Colson, Pierre mailto [Université de Liège - ULg > Département de chimie (sciences) > Département de chimie (sciences) >]
Heinen, Ernst mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine >]
Elmoualij, Benaïssa mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie humaine >]
2005
Biochemical and Biophysical Research Communications
Academic Press
331
4
894-901
Yes (verified by ORBi)
International
0006-291X
1090-2104
San Diego
CA
[en] Cell Line, Tumor ; Circular Dichroism ; Humans ; Lipid Metabolism ; Membrane Fusion ; Models, Molecular ; Peptide Fragments/chemistry/metabolism ; Prions/chemistry/metabolism ; Protein Binding ; Protein Structure, Secondary ; Spectrophotometry, Ultraviolet
[en] Prion diseases are fatal neurodegenerative disorders characterized by the accumulation in the brain of an abnormally misfolded, protease-resistant, and beta-sheet rich pathogenic isoform (PrP(SC)) of the cellular prion protein (PrP(C)). In the present work, we were interested to study the mode of prion protein interaction with the membrane using the 106-126 peptide and small unilamellar lipid vesicles as model. As previously demonstrated, we showed by MTS assay that PrP 106-126 induces alterations in the human neuroblastoma SH-SY5Y cell line. We demonstrated for the first time by lipid-mixing assay and by the liposome vesicle leakage test that PrP 106-126, a non-tilted peptide, induces liposome fusion thus a potential cell membrane destabilization, as supported by membrane integrity assay (LDH). By circular dichroism (CD) analysis we showed that the fusogenic property of PrP 106-126 in the presence of liposome is associated with a predominantly beta-sheet structure. These data suggest that the fusogenic property associated with a predominant beta-sheet structure exhibited by the prion peptides contributes to the neurotoxicity of these peptides by destabilizing cellular membranes. The latter might be attached at the membrane surface in a parallel orientation as shown by molecular modeling.
Researchers ; Professionals
http://hdl.handle.net/2268/63493
also: http://hdl.handle.net/2268/26235
10.1016/j.bbrc.2005.04.012

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