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Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics

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  • Aaron M Streets
  • Yannick Sourigues
  • Ron R Kopito
  • Ronald Melki
  • Stephen R Quake

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, in vitro. 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.

Suggested Citation

  • Aaron M Streets & Yannick Sourigues & Ron R Kopito & Ronald Melki & Stephen R Quake, 2013. "Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics," PLOS ONE, Public Library of Science, vol. 8(1), pages 1-10, January.
    • Handle: RePEc:plo:pone00:0054541
    DOI: 10.1371/journal.pone.0054541
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    References listed on IDEAS

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    1. Montserrat Arrasate & Siddhartha Mitra & Erik S. Schweitzer & Mark R. Segal & Steven Finkbeiner, 2004. "Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death," Nature, Nature, vol. 431(7010), pages 805-810, October.
    2. Monica Bucciantini & Elisa Giannoni & Fabrizio Chiti & Fabiana Baroni & Lucia Formigli & Jesús Zurdo & Niccolò Taddei & Giampietro Ramponi & Christopher M. Dobson & Massimo Stefani, 2002. "Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases," Nature, Nature, vol. 416(6880), pages 507-511, April.
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