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Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

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  • Ricardo M. P. da Silva

    (Simpson Querrey Institute for BioNanotechnology (SQI), Northwestern University
    Laboratory of Macromolecular and Organic Chemistry and Institute for Complex Molecular Systems, Eindhoven University of Technology
    Craniofacial Development & Stem Cell Biology, King's College London)

  • Daan van der Zwaag

    (Laboratory of Macromolecular and Organic Chemistry and Institute for Complex Molecular Systems, Eindhoven University of Technology)

  • Lorenzo Albertazzi

    (Laboratory of Macromolecular and Organic Chemistry and Institute for Complex Molecular Systems, Eindhoven University of Technology
    Nanoscopy for Nanomedicine Group, Institute for Bioengineering of Catalonia (IBEC))

  • Sungsoo S. Lee

    (Northwestern University)

  • E. W. Meijer

    (Laboratory of Macromolecular and Organic Chemistry and Institute for Complex Molecular Systems, Eindhoven University of Technology)

  • Samuel I. Stupp

    (Simpson Querrey Institute for BioNanotechnology (SQI), Northwestern University
    Northwestern University
    Northwestern University
    Northwestern University)

Abstract

The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.

Suggested Citation

  • Ricardo M. P. da Silva & Daan van der Zwaag & Lorenzo Albertazzi & Sungsoo S. Lee & E. W. Meijer & Samuel I. Stupp, 2016. "Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres," Nature Communications, Nature, vol. 7(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11561
    DOI: 10.1038/ncomms11561
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