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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Amyloids of Alpha-Synuclein Affect the Structure and Dynamics of Supported Lipid Bilayers</title><author><name sortKey="Iyer, Aditya" sort="Iyer, Aditya" uniqKey="Iyer A" first="Aditya" last="Iyer">Aditya Iyer</name><affiliation><nlm:aff id="aff1">Nanoscale Biophysics Group, FOM Institute AMOLF, Amsterdam, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Petersen, Nils O" sort="Petersen, Nils O" uniqKey="Petersen N" first="Nils O." last="Petersen">Nils O. Petersen</name><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff3">Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada</nlm:aff></affiliation></author><author><name sortKey="Claessens, Mireille M A E" sort="Claessens, Mireille M A E" uniqKey="Claessens M" first="Mireille M. A. E." last="Claessens">Mireille M. A. E. Claessens</name><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Subramaniam, Vinod" sort="Subramaniam, Vinod" uniqKey="Subramaniam V" first="Vinod" last="Subramaniam">Vinod Subramaniam</name><affiliation><nlm:aff id="aff1">Nanoscale Biophysics Group, FOM Institute AMOLF, Amsterdam, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24940776</idno><idno type="pmc">4070068</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4070068</idno><idno type="RBID">PMC:4070068</idno><idno type="doi">10.1016/j.bpj.2014.05.001</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000521</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000521</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Amyloids of Alpha-Synuclein Affect the Structure and Dynamics of Supported Lipid Bilayers</title><author><name sortKey="Iyer, Aditya" sort="Iyer, Aditya" uniqKey="Iyer A" first="Aditya" last="Iyer">Aditya Iyer</name><affiliation><nlm:aff id="aff1">Nanoscale Biophysics Group, FOM Institute AMOLF, Amsterdam, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Petersen, Nils O" sort="Petersen, Nils O" uniqKey="Petersen N" first="Nils O." last="Petersen">Nils O. Petersen</name><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff3">Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada</nlm:aff></affiliation></author><author><name sortKey="Claessens, Mireille M A E" sort="Claessens, Mireille M A E" uniqKey="Claessens M" first="Mireille M. A. E." last="Claessens">Mireille M. A. E. Claessens</name><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Subramaniam, Vinod" sort="Subramaniam, Vinod" uniqKey="Subramaniam V" first="Vinod" last="Subramaniam">Vinod Subramaniam</name><affiliation><nlm:aff id="aff1">Nanoscale Biophysics Group, FOM Institute AMOLF, Amsterdam, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</nlm:aff></affiliation></author></analytic><series><title level="j">Biophysical Journal</title><idno type="ISSN">0006-3495</idno><idno type="eISSN">1542-0086</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Interactions of monomeric alpha-synuclein (<italic>α</italic>S) with lipid membranes have been suggested to play an important role in initiating aggregation of <italic>α</italic>S. We have systematically analyzed the distribution and self-assembly of monomeric <italic>α</italic>S on supported lipid bilayers. We observe that at protein/lipid ratios higher than 1:10, <italic>α</italic>S forms micrometer-sized clusters, leading to observable membrane defects and decrease in lateral diffusion of both lipids and proteins. An <italic>α</italic>S deletion mutant lacking amino-acid residues 71–82 binds to membranes, but does not observably affect membrane integrity. Although this deletion mutant cannot form amyloid, significant amyloid formation is observed in the wild-type <italic>α</italic>S clusters. These results suggest that the process of amyloid formation, rather than binding of <italic>α</italic>S on membranes, is crucial in compromising membrane integrity.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Biophys J</journal-id><journal-id journal-id-type="iso-abbrev">Biophys. J</journal-id><journal-title-group><journal-title>Biophysical Journal</journal-title></journal-title-group><issn pub-type="ppub">0006-3495</issn><issn pub-type="epub">1542-0086</issn><publisher><publisher-name>The Biophysical Society</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">24940776</article-id><article-id pub-id-type="pmc">4070068</article-id><article-id pub-id-type="publisher-id">S0006-3495(14)00463-9</article-id><article-id pub-id-type="doi">10.1016/j.bpj.2014.05.001</article-id><article-categories><subj-group subj-group-type="heading"><subject>Membranes</subject></subj-group></article-categories><title-group><article-title>Amyloids of Alpha-Synuclein Affect the Structure and Dynamics of Supported Lipid Bilayers</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Iyer</surname><given-names>Aditya</given-names></name><xref rid="aff1" ref-type="aff">†</xref><xref rid="aff2" ref-type="aff">‡</xref></contrib><contrib contrib-type="author"><name><surname>Petersen</surname><given-names>Nils O.</given-names></name><xref rid="aff2" ref-type="aff">‡</xref><xref rid="aff3" ref-type="aff">§</xref></contrib><contrib contrib-type="author"><name><surname>Claessens</surname><given-names>Mireille M.A.E.</given-names></name><xref rid="aff2" ref-type="aff">‡</xref></contrib><contrib contrib-type="author"><name><surname>Subramaniam</surname><given-names>Vinod</given-names></name><email>subramaniam@amolf.nl</email><xref rid="aff1" ref-type="aff">†</xref><xref rid="aff2" ref-type="aff">‡</xref><xref rid="cor1" ref-type="corresp">∗</xref></contrib></contrib-group><aff id="aff1"><label>†</label>Nanoscale Biophysics Group, FOM Institute AMOLF, Amsterdam, The Netherlands</aff><aff id="aff2"><label>‡</label>Nanobiophysics Group, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands</aff><aff id="aff3"><label>§</label>Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada</aff><author-notes><corresp id="cor1"><label>∗</label>Corresponding author <email>subramaniam@amolf.nl</email></corresp></author-notes><pub-date pub-type="ppub"><day>17</day><month>6</month><year>2014</year></pub-date><volume>106</volume><issue>12</issue><fpage>2585</fpage><lpage>2594</lpage><history><date date-type="received"><day>31</day><month>1</month><year>2014</year></date><date date-type="accepted"><day>1</day><month>5</month><year>2014</year></date></history><permissions><copyright-statement>© 2014 by the Biophysical Society.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>Biophysical Society</copyright-holder></permissions><abstract><p>Interactions of monomeric alpha-synuclein (<italic>α</italic>S) with lipid membranes have been suggested to play an important role in initiating aggregation of <italic>α</italic>S. We have systematically analyzed the distribution and self-assembly of monomeric <italic>α</italic>S on supported lipid bilayers. We observe that at protein/lipid ratios higher than 1:10, <italic>α</italic>S forms micrometer-sized clusters, leading to observable membrane defects and decrease in lateral diffusion of both lipids and proteins. An <italic>α</italic>S deletion mutant lacking amino-acid residues 71–82 binds to membranes, but does not observably affect membrane integrity. Although this deletion mutant cannot form amyloid, significant amyloid formation is observed in the wild-type <italic>α</italic>S clusters. These results suggest that the process of amyloid formation, rather than binding of <italic>α</italic>S on membranes, is crucial in compromising membrane integrity.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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