Self-Assembly of Protein Fibrils into Suprafibrillar Aggregates: Bridging the Nano- and Mesoscale

Slav Angelov Semerdzhiev, D.R. Dekker, Vinod Subramaniam, Mireille Maria Anna Elisabeth Claessens

Research output: Contribution to journalArticleAcademicpeer-review

32 Citations (Scopus)

Abstract

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 languageUndefined
Pages (from-to)5543-5551
JournalACS nano
Volume8
Issue number6
DOIs
Publication statusPublished - 2014

Keywords

  • METIS-303799
  • IR-94879

Cite this

Semerdzhiev, Slav Angelov ; Dekker, D.R. ; Subramaniam, Vinod ; Claessens, Mireille Maria Anna Elisabeth. / Self-Assembly of Protein Fibrils into Suprafibrillar Aggregates: Bridging the Nano- and Mesoscale. In: ACS nano. 2014 ; Vol. 8, No. 6. pp. 5543-5551.
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abstract = "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",
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Self-Assembly of Protein Fibrils into Suprafibrillar Aggregates: Bridging the Nano- and Mesoscale. / Semerdzhiev, Slav Angelov; Dekker, D.R.; Subramaniam, Vinod; Claessens, Mireille Maria Anna Elisabeth.

In: ACS nano, Vol. 8, No. 6, 2014, p. 5543-5551.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Claessens, Mireille Maria Anna Elisabeth

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AB - 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

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