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Interaction of the prion protein fragment PrP 185–206 with biological membranes: effect on membrane permeability
Author(s) -
Sonkina Sabina,
Tukhfatullina Ilnor I.,
BensenyCases Núria,
Ionov Maksim,
Bryszewska Maria,
Salakhutdinov Bakhtiyar A.,
Cladera Josep
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1247
Subject(s) - membrane , peptide , chemistry , biophysics , membrane permeability , permeability (electromagnetism) , cell membrane , amyloid (mycology) , static electricity , biochemistry , biology , inorganic chemistry , electrical engineering , engineering
Amyloids are proteinaceous aggregates related to the so‐called conformational diseases, such as Alzheimer's and prion diseases. The cytotoxicity of amyloids may be related to the interaction of the amiloidogenic peptides or proteins with the cell membrane. In order to gain information on the physico‐chemical effects of amyloids on membranes, we have studied the interaction of the human prion amyloidogenic fragment PrP 185–206 with negatively charged model membranes. The results show that the peptide causes the destabilization of the membrane, making it permeable to potassium ions and to charged organic compounds. This effect correlates with the interaction of the peptide with the membrane, causing a variation in the magnitude of the electrostatic surface and dipole membrane potentials. This effect on the electrostatic properties of the membranes may help explaining the observed permeability: a neutralization of the surface negative charge and a decrease of the inside‐positive dipole potential would facilitate the translocation of positive ions. The structural analysis of the peptide in the presence of model membranes reveals that it adopts a predominantly unordered structure without any signs of amyloid formation. The results may be relevant in relation to the recently described cell toxic capacity of the peptide. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.