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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>
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<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>
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