title: Interactions between the conserved hydrophobic region of the prion protein and dodecylphosphocholine micelles.
abstract: The three-dimensional structure of PrP110-136, a peptide encompassing the conserved hydrophobic region of the human prion protein, has been determined at high resolution in dodecylphosphocholine micelles by NMR. The results support the conclusion that the (Ctm)PrP, a transmembrane form of the prion protein, adopts a different conformation than the reported structures of the normal prion protein determined in solution. Paramagnetic relaxation enhancement studies with gadolinium-diethylenetriaminepentaacetic acid indicated that the conserved hydrophobic region peptide is not inserted symmetrically in the micelle, thus suggesting the presence of a guanidium-phosphate ion pair involving the side chain of the terminal arginine and the detergent headgroup. Titration of dodecylphosphocholine into a solution of PrP110-136 revealed the presence of a surface-bound species. In addition, paramagnetic probes located the surface-bound peptide somewhere below the micelle-water interface when using the inserted helix as a positional reference. This localization of the unknown population would allow a similar ion pair interaction.
authors: Centre for Vaccine Evaluation, Biologics and Genetic Therapies Directorate, Health Canada, Ottawa, Ontario K1A 0K9, Canada.
authors: Simon
authors: S
authors: Sauvé
authors: Daniel
authors: D
authors: Buijs
authors: Geneviève
authors: G
authors: Gingras
authors: Yves
authors: Y
authors: Aubin
mesh_terms: D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000737:chemistry; D011328:Prions / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D008823:Micelles; D010455:Peptides; D011328:Prions; D010767:Phosphorylcholine; C028810:dodecylphosphocholine