Prion protein structure is affected by pH‐dependent interaction with membranes: A study in a model system
2007; Wiley; Volume: 582; Issue: 2 Linguagem: Inglês
10.1016/j.febslet.2007.12.003
ISSN1873-3468
AutoresFrancesca Re, Silvia Sesana, Alberto Barbiroli, Francesco Bonomi, Emanuela Cazzaniga, Elena Lonati, Alessandra Bulbarelli, Massimo Masserini,
Tópico(s)Infectious Encephalopathies and Encephalitis
ResumoInteraction 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.
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