Interaction of full length recombinant hamster prion protein with liposomes mimicking lipid rafts or non-raft membrane regions was studied by circular dichroism, chemical cross-linking and sucrose gradient ultracentrifugation. At pH 7.0, the protein bound palmitoyloleoylphosphatidylcholine/cholesterol/sphingomyelin/monosialoganglioside GM1 (GM1) ganglioside liposomes but not palmitoyloleoylphosphatidylcholine alone (bound/free = 0.33 and 0.01, respectively), maintaining the native α-helical structure and monomeric form. At pH 5.0, though still binding to quaternary mixtures, in particular GM1, the protein bound also to palmitoyloleoylphosphatidylcholine (bound/free 0.35) becoming unfolded and oligomeric. The pH-dependent interaction with raft or non-raft membranes might have implication in vivo, by stabilizing or destabilizing the protein. © 2007 Federation of European Biochemical Societies.
Re, F., Sesana, M.S., Barbiroli, A., Bonomi, F., Cazzaniga, E., Lonati, E.R., et al. (2008). Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system. FEBS LETTERS, 582(2), 215-220.
Citazione: | Re, F., Sesana, M.S., Barbiroli, A., Bonomi, F., Cazzaniga, E., Lonati, E.R., et al. (2008). Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system. FEBS LETTERS, 582(2), 215-220. |
Tipo: | Articolo in rivista - Articolo scientifico |
Carattere della pubblicazione: | Scientifica |
Titolo: | Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system |
Autori: | Re, F; Sesana, MS; Barbiroli, A; Bonomi, F; Cazzaniga, E; Lonati, ER; Bulbarelli, A; Masserini, ME |
Autori: | |
Data di pubblicazione: | 2008 |
Lingua: | English |
Rivista: | FEBS LETTERS |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/j.febslet.2007.12.003 |
Appare nelle tipologie: | 01 - Articolo su rivista |