PrP(106-126) does not interact with membranes under physiological conditions

Detalhes bibliográficos
Autor(a) principal: Henriques, Sónia Troeira
Data de Publicação: 2008
Outros Autores: Pattenden, Leonard Keith, Aguilar, Marie-Isabel, Castanho, Miguel A. R. B.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/7260
Resumo: © 2008 by the Biophysical Society
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spelling PrP(106-126) does not interact with membranes under physiological conditions© 2008 by the Biophysical SocietyTransmissible 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.This work was supported by a grant from Fundação para a Ciência e Tecnologia (SFRH/BD/14337/2003 to S.T.H.). The International Union of Biochemistry and Molecular Biology is acknowledged for financial support to S.T.H. for a short-term visit to the Marie-Isabel Aguilar laboratory at Monash University, Victoria, Australia. The support of the Australian Research Council and the Potter Foundation is gratefully acknowledged.Biophysical SocietyRepositório da Universidade de LisboaHenriques, Sónia TroeiraPattenden, Leonard KeithAguilar, Marie-IsabelCastanho, Miguel A. R. B.2012-11-21T15:12:57Z20082008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/7260engBiophysical Journal 95(4) 1877–1889, August 20080006-3495hhtp://dx.doi.org/10.1529/biophysj.108.131458info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T15:50:17Zoai:repositorio.ul.pt:10451/7260Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:32:06.903642Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv PrP(106-126) does not interact with membranes under physiological conditions
title PrP(106-126) does not interact with membranes under physiological conditions
spellingShingle PrP(106-126) does not interact with membranes under physiological conditions
Henriques, Sónia Troeira
title_short PrP(106-126) does not interact with membranes under physiological conditions
title_full PrP(106-126) does not interact with membranes under physiological conditions
title_fullStr PrP(106-126) does not interact with membranes under physiological conditions
title_full_unstemmed PrP(106-126) does not interact with membranes under physiological conditions
title_sort PrP(106-126) does not interact with membranes under physiological conditions
author Henriques, Sónia Troeira
author_facet Henriques, Sónia Troeira
Pattenden, Leonard Keith
Aguilar, Marie-Isabel
Castanho, Miguel A. R. B.
author_role author
author2 Pattenden, Leonard Keith
Aguilar, Marie-Isabel
Castanho, Miguel A. R. B.
author2_role author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Henriques, Sónia Troeira
Pattenden, Leonard Keith
Aguilar, Marie-Isabel
Castanho, Miguel A. R. B.
description © 2008 by the Biophysical Society
publishDate 2008
dc.date.none.fl_str_mv 2008
2008-01-01T00:00:00Z
2012-11-21T15:12:57Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/7260
url http://hdl.handle.net/10451/7260
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biophysical Journal 95(4) 1877–1889, August 2008
0006-3495
hhtp://dx.doi.org/10.1529/biophysj.108.131458
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Biophysical Society
publisher.none.fl_str_mv Biophysical Society
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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instacron:RCAAP
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