Abstract:
:Transmissible spongiform encephalopathies are neurodegenerative diseases characterized by the accumulation of an abnormal isoform of the prion protein PrP(Sc). Its fragment 106-126 has been reported to maintain most of the pathological features of PrP(Sc), and a role in neurodegeneration has been proposed based on the modulation of membrane properties and channel formation. The ability of PrP(Sc) to modulate membranes and/or form channels in membranes has not been clearly demonstrated; however, if these processes are important, peptide-membrane interactions would be a key feature in the toxicity of PrP(Sc). In this work, the interaction of PrP(106-126) with model membranes comprising typical lipid identities, as well as more specialized lipids such as phosphatidylserine and GM1 ganglioside, was examined using surface plasmon resonance and fluorescence methodologies. This comprehensive study examines different parameters relevant to characterization of peptide-membrane interactions, including membrane charge, viscosity, lipid composition, pH, and ionic strength. We report that PrP(106-126) has a low affinity for lipid membranes under physiological conditions without evidence of membrane disturbances. Membrane insertion and leakage occur only under conditions in which strong electrostatic interactions operate. These results support the hypothesis that the physiological prion protein PrP(C) mediates PrP(106-126) toxic effects in neuronal cells.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Henriques ST,Pattenden LK,Aguilar MI,Castanho MAdoi
10.1529/biophysj.108.131458subject
Has Abstractpub_date
2008-08-01 00:00:00pages
1877-89issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(08)70147-4journal_volume
95pub_type
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