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 in | Nature communications Vol. 7; no. 1; pp. 11561 - 10 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
19.05.2016
Nature Publishing Group Nature Portfolio |
| Subjects | |
| Online Access | Get full text |
| ISSN | 2041-1723 2041-1723 |
| DOI | 10.1038/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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| Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 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 |