Self-assembly of protein fibrils into suprafibrillar aggregates: bridging the nano- and mesoscale

Slav A Semerdzhiev, Dirk R Dekker, Vinod Subramaniam, Mireille M A E Claessens

    Research output: Contribution to JournalArticleAcademicpeer-review


    We report on in vitro self-assembly of nanometer-sized α-synuclein amyloid fibrils into well-defined micrometer-sized suprafibrillar aggregates with sheet-like or cylindrical morphology depending on the ionic strength of the solution. The cylindrical suprafibrillar structures are heavily hydrated, suggesting swollen gel-like particles. In contrast to higher order structures formed by other negatively charged biopolymers, multivalent ions are not required for the suprafibrillar aggregates to form. Their formation is induced by both mono- and divalent counterions. The self-assembly process is not mediated by protein-specific interactions but rather by the cooperative action of long-range electrostatic repulsion and short-range attraction. Understanding the mechanism driving the self-assembly might give us valuable insight into the pathological formation of fibrillar superstructures such as Lewy bodies and neurites-distinct signatures of Parkinson's disease-and will open the possibility to utilize the self-assembly process for the design of novel fibril-based smart nanostructured materials.

    Original languageEnglish
    Pages (from-to)5543-51
    Number of pages9
    JournalACS Nano
    Issue number6
    Publication statusPublished - 24 Jun 2014


    • Amyloid
    • Binding Sites
    • Humans
    • Hydrogen-Ion Concentration
    • Ions
    • Lewy Bodies
    • Microscopy, Atomic Force
    • Mutation
    • Nanotechnology
    • Osmolar Concentration
    • Parkinson Disease
    • Protein Structure, Secondary
    • Proteins
    • Solutions
    • Static Electricity
    • Temperature
    • alpha-Synuclein
    • Journal Article
    • Research Support, Non-U.S. Gov't


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