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., Barbiroli, A., Bonomi, F., Cazzaniga, E., Lonati, E., 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 [10.1016/j.febslet.2007.12.003].
Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system
RE, FRANCESCA;SESANA, MARIA SILVIA;CAZZANIGA, EMANUELA;LONATI, ELENA RITA;BULBARELLI, ALESSANDRA;MASSERINI, MASSIMO ERNESTO
2008
Abstract
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.
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