Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles

Anja N D Stefanovic, Mireille M A E Claessens, Christian Blum, Vinod Subramaniam

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed.

    Original languageEnglish
    Pages (from-to)2257-62
    Number of pages6
    JournalSmall
    Volume11
    Issue number19
    DOIs
    Publication statusPublished - 2015

    Keywords

    • Amyloid
    • Fluorescent Dyes
    • Nanoparticles
    • Phosphatidylglycerols
    • Protein Multimerization
    • Unilamellar Liposomes
    • alpha-Synuclein
    • Journal Article
    • Research Support, Non-U.S. Gov't

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