Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics
Identifieur interne : 000811 ( Pmc/Curation ); précédent : 000810; suivant : 000812Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics
Auteurs : Aaron M. Streets [États-Unis] ; Yannick Sourigues [France] ; Ron R. Kopito [États-Unis] ; Ronald Melki [France] ; Stephen R. Quake [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2013.
Abstract
An apparatus that combines dynamic light scattering and Thioflavin T fluorescence detection is used to simultaneously probe fibril formation in polyglutamine peptides, the aggregating subunit associated with Huntington's disease,
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DOI: 10.1371/journal.pone.0054541
PubMed: 23349924
PubMed Central: 3547910
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Streets</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Applied Physics, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Applied Physics, Stanford University, Stanford, California</wicri:regionArea></affiliation></author><author><name sortKey="Sourigues, Yannick" sort="Sourigues, Yannick" uniqKey="Sourigues Y" first="Yannick" last="Sourigues">Yannick Sourigues</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Kopito, Ron R" sort="Kopito, Ron R" uniqKey="Kopito R" first="Ron R." last="Kopito">Ron R. 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Quake</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Applied Physics, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Applied Physics, Stanford University, Stanford, California</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff4"><addr-line>Department of Bioengineering, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Bioengineering, Stanford University, Stanford, California</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff5"><addr-line>Howard Hughes Medical Institute, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Howard Hughes Medical Institute, Stanford University, Stanford, California</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">23349924</idno><idno type="pmc">3547910</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3547910</idno><idno type="RBID">PMC:3547910</idno><idno type="doi">10.1371/journal.pone.0054541</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000814</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000814</idno><idno type="wicri:Area/Pmc/Curation">000811</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000811</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics</title><author><name sortKey="Streets, Aaron M" sort="Streets, Aaron M" uniqKey="Streets A" first="Aaron M." last="Streets">Aaron M. Streets</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Applied Physics, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Applied Physics, Stanford University, Stanford, California</wicri:regionArea></affiliation></author><author><name sortKey="Sourigues, Yannick" sort="Sourigues, Yannick" uniqKey="Sourigues Y" first="Yannick" last="Sourigues">Yannick Sourigues</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Kopito, Ron R" sort="Kopito, Ron R" uniqKey="Kopito R" first="Ron R." last="Kopito">Ron R. Kopito</name><affiliation wicri:level="1"><nlm:aff id="aff3"><addr-line>Department of Biology, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biology, Stanford University, Stanford, California</wicri:regionArea></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Quake, Stephen R" sort="Quake, Stephen R" uniqKey="Quake S" first="Stephen R." last="Quake">Stephen R. Quake</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Department of Applied Physics, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Applied Physics, Stanford University, Stanford, California</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff4"><addr-line>Department of Bioengineering, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Bioengineering, Stanford University, Stanford, California</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff5"><addr-line>Howard Hughes Medical Institute, Stanford University, Stanford, California, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Howard Hughes Medical Institute, Stanford University, Stanford, California</wicri:regionArea></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>An apparatus that combines dynamic light scattering and Thioflavin T fluorescence detection is used to simultaneously probe fibril formation in polyglutamine peptides, the aggregating subunit associated with Huntington's disease, <italic>in vitro</italic>. Huntington's disease is a neurodegenerative disorder in a class of human pathologies that includes Alzheimer's and Parkinson's disease. These pathologies are all related by the propensity of their associated protein or polypeptide to form insoluble, β-sheet rich, amyloid fibrils. Despite the wide range of amino acid sequence in the aggregation prone polypeptides associated with these diseases, the resulting amyloids display strikingly similar physical structure, an observation which suggests a physical basis for amyloid fibril formation. Thioflavin T fluorescence reports β-sheet fibril content while dynamic light scattering measures particle size distributions. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">PLoS One</journal-id><journal-id journal-id-type="iso-abbrev">PLoS ONE</journal-id><journal-id journal-id-type="publisher-id">plos</journal-id><journal-id journal-id-type="pmc">plosone</journal-id><journal-title-group><journal-title>PLoS ONE</journal-title></journal-title-group><issn pub-type="epub">1932-6203</issn><publisher><publisher-name>Public Library of Science</publisher-name><publisher-loc>San Francisco, USA</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23349924</article-id><article-id pub-id-type="pmc">3547910</article-id><article-id pub-id-type="publisher-id">PONE-D-12-16061</article-id><article-id pub-id-type="doi">10.1371/journal.pone.0054541</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="Discipline-v2"><subject>Biology</subject><subj-group><subject>Biochemistry</subject><subj-group><subject>Proteins</subject><subj-group><subject>Protein Interactions</subject><subject>Protein Structure</subject></subj-group></subj-group></subj-group><subj-group><subject>Genetics</subject><subj-group><subject>Human Genetics</subject><subj-group><subject>Autosomal Dominant</subject><subj-group><subject>Huntington Disease</subject></subj-group></subj-group></subj-group></subj-group></subj-group><subj-group subj-group-type="Discipline-v2"><subject>Chemistry</subject><subj-group><subject>Polymer Chemistry</subject><subj-group><subject>Polymerization</subject></subj-group></subj-group></subj-group><subj-group subj-group-type="Discipline-v2"><subject>Physics</subject><subj-group><subject>Biophysics</subject><subj-group><subject>Macromolecular Assemblies</subject></subj-group></subj-group><subj-group><subject>Condensed-Matter Physics</subject><subj-group><subject>Optics</subject><subject>Phase Transformation</subject></subj-group></subj-group></subj-group></article-categories><title-group><article-title>Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics</article-title><alt-title alt-title-type="running-head">DLS and THT Investigation of Fibril Growth</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Streets</surname><given-names>Aaron M.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>¤</sup></xref></contrib><contrib contrib-type="author"><name><surname>Sourigues</surname><given-names>Yannick</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kopito</surname><given-names>Ron R.</given-names></name><xref ref-type="aff" rid="aff3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Melki</surname><given-names>Ronald</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Quake</surname><given-names>Stephen R.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="aff" rid="aff4"><sup>4</sup></xref><xref ref-type="aff" rid="aff5"><sup>5</sup></xref><xref ref-type="corresp" rid="cor1"><sup>*</sup></xref></contrib></contrib-group><aff id="aff1"><label>1</label><addr-line>Department of Applied Physics, Stanford University, Stanford, California, United States of America</addr-line></aff><aff id="aff2"><label>2</label><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></aff><aff id="aff3"><label>3</label><addr-line>Department of Biology, Stanford University, Stanford, California, United States of America</addr-line></aff><aff id="aff4"><label>4</label><addr-line>Department of Bioengineering, Stanford University, Stanford, California, United States of America</addr-line></aff><aff id="aff5"><label>5</label><addr-line>Howard Hughes Medical Institute, Stanford University, Stanford, California, United States of America</addr-line></aff><contrib-group><contrib contrib-type="editor"><name><surname>Georgakoudi</surname><given-names>Irene</given-names></name><role>Editor</role><xref ref-type="aff" rid="edit1"></xref></contrib></contrib-group><aff id="edit1"><addr-line>Tufts University, United States of America</addr-line></aff><author-notes><corresp id="cor1">* E-mail: <email>quake@stanford.edu</email></corresp><fn fn-type="conflict"><p><bold>Competing Interests: </bold>The authors have declared that no competing interests exist.</p></fn><fn fn-type="con"><p>Edited the manuscript: RRK RM SRQ. Conceived and designed the experiments: AMS RRK RM SRQ. Performed the experiments: AMS. Analyzed the data: AMS RRK RM SRQ. Contributed reagents/materials/analysis tools: YS RRK RM SRQ. Wrote the paper: AMS.</p></fn><fn id="fn1" fn-type="current-aff"><label>¤</label><p>Current address: Peking University, Beijing, China</p></fn></author-notes><pub-date pub-type="collection"><year>2013</year></pub-date><pub-date pub-type="epub"><day>17</day><month>1</month><year>2013</year></pub-date><volume>8</volume><issue>1</issue><elocation-id>e54541</elocation-id><history><date date-type="received"><day>3</day><month>6</month><year>2012</year></date><date date-type="accepted"><day>13</day><month>12</month><year>2012</year></date></history><permissions><copyright-year>2013</copyright-year><copyright-holder>Streets et al</copyright-holder><license><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</license-p></license></permissions><abstract><p>An apparatus that combines dynamic light scattering and Thioflavin T fluorescence detection is used to simultaneously probe fibril formation in polyglutamine peptides, the aggregating subunit associated with Huntington's disease, <italic>in vitro</italic>. Huntington's disease is a neurodegenerative disorder in a class of human pathologies that includes Alzheimer's and Parkinson's disease. These pathologies are all related by the propensity of their associated protein or polypeptide to form insoluble, β-sheet rich, amyloid fibrils. Despite the wide range of amino acid sequence in the aggregation prone polypeptides associated with these diseases, the resulting amyloids display strikingly similar physical structure, an observation which suggests a physical basis for amyloid fibril formation. Thioflavin T fluorescence reports β-sheet fibril content while dynamic light scattering measures particle size distributions. The combined techniques allow elucidation of complex aggregation kinetics and are used to reveal multiple stages of amyloid fibril formation.</p></abstract><funding-group><funding-statement>AMS was supported by the Stanford DARE Fellowship. YS and RM were supported by the Agence Nationale de la Recherche (ANR-08-NEUR-001-01 and ANR-09-MNPS-013-01) and the CNRS. This work was also supported by grants from the NINDS, the Human Frontier Science Program, and the Huntington's Disease Society of America. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.</funding-statement></funding-group><counts><page-count count="10"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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