Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/7260
Título: PrP(106-126) does not interact with membranes under physiological conditions
Autor: Henriques, Sónia Troeira
Pattenden, Leonard Keith
Aguilar, Marie-Isabel
Castanho, Miguel A. R. B.
Data: 2008
Editora: Biophysical Society
Citação: Biophysical Journal Volume 95 August 2008 1877–1889
Resumo: Transmissible spongiform encephalopathies are neurodegenerative diseases characterized by the accumulation of an abnormal isoform of the prion protein PrPSc. Its fragment 106-126 has been reported to maintain most of the pathological features of PrPSc, and a role in neurodegeneration has been proposed based on the modulation of membrane properties and channel formation. The ability of PrPSc 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 PrPSc. 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 peptidemembrane 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 PrPC mediates PrP(106-126) toxic effects in neuronal cells.
Descrição: © 2008 by the Biophysical Society
Peer review: yes
URI: hhtp://dx.doi.org/10.1529/biophysj.108.131458
ISSN: 0006-3495
Aparece nas colecções:IMM - Artigos em Revistas Internacionais

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