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

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 biomedic...

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Published inNature communications Vol. 7; no. 1; pp. 11561 - 10
Main Authors da Silva, Ricardo M. P., van der Zwaag, Daan, Albertazzi, Lorenzo, Lee, Sungsoo S., Meijer, E. W., Stupp, Samuel I.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 19.05.2016
Nature Publishing Group
Nature Portfolio
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ISSN2041-1723
2041-1723
DOI10.1038/ncomms11561

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Summary: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. Dynamic behaviour in supramolecular systems is an important aspect of their functionality. Here, the authors use stochastic optical reconstruction microscopy to unveil structural diversity in self-assembled peptide amphiphile nanofibres, with potential relevance to biomedical applications.
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Marie Curie FP7-PEOPLE-IOF program
FG02-00ER45810
European Research Council (ERC)
Dutch Ministry of Education, Culture and Science (Gravity program)
USDOE Office of Science (SC), Basic Energy Sciences (BES)
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms11561