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.

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, F
;
Sesana, MS;Bonomi, F;Cazzaniga, E;Lonati, ER;Bulbarelli, A;Masserini, ME
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.
Articolo in rivista - Articolo scientifico
Circular dichroism; Lipid rafts; Liposomes; Prion protein; Protein structure;
English
2008
582
2
215
220
none
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].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/5152
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