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Nano Research 2015, 8(6): 1822-1833 https://doi.org/10.1007/s12274-014-0683-9
Research Article | Open Access | Issue | Published: 28 March 2015

Tracking morphologies at the nanoscale: Self-assembly of an amphiphilic designer peptide into a double helix superstructure

Show Author's Information Karin Kornmueller1,  Ilse Letofsky-Papst2,  Kerstin Gradauer1,  Christian Mikl1,  Fernando Cacho-Nerin3,†,  Mario Leypold4,  Walter Keller5,  Gerd Leitinger6,7,  Heinz Amenitsch3,  Ruth Prassl1( )
Institute of BiophysicsMedical University of GrazBioTechMed-Graz8010Graz, Austria
Institute for Electron Microscopy and NanoanalysisGraz University of Technology and Graz Centre for Electron Microscopy8010Graz, Austria
Institute of Inorganic ChemistryGraz University of Technology8010Graz, Austria
Institute of Organic ChemistryGraz University of Technology8010Graz, Austria
Institute for Molecular BiosciencesKarl-Franzens-University Graz8010Graz, Austria
Research Unit Electron Microscopic TechniquesInstitute of Cell BiologyHistology and EmbryologyMedical University of Graz8010Graz, Austria
Center for Medical ResearchMedical University of Graz8010Graz, Austria

† Present address: Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom

Keywords:
self-assembly, TEM, spectroscopy, double helix, amphiphilic designer peptide, SAXS
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Kornmueller K, Letofsky-Papst I, Gradauer K, et al. Tracking morphologies at the nanoscale: Self-assembly of an amphiphilic designer peptide into a double helix superstructure. Nano Research, 2015, 8(6): 1822-1833. https://doi.org/10.1007/s12274-014-0683-9
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Abstract Full text Electronic supplementary material About this article

Hierarchical self-assembly is a fundamental principle in nature, which gives rise to astonishing supramolecular architectures that are an inspiration for the development of innovative materials in nanotechnology. Here, we present the unique structure of a cone-shaped amphiphilic designer peptide. While tracking its concentration-dependent morphologies, we observed elongated bilayered single tapes at the beginning of the assembly process, which further developed into novel double-helix-like superstructures at high concentrations. This architecture is characterized by a tight intertwisting of two individual helices, resulting in a periodic pitch size over their total lengths of several hundred nanometers. Solution X-ray scattering data revealed a marked 2-layered internal organization. All these characteristics remained unaltered for the investigated period of almost three months. In their collective morphology, the assemblies are integrated into a network with hydrogel characteristics. Such a peptide-based structure holds promise as a building block for next-generation nanostructured biomaterials.


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Electronic supplementary material
About this article

Tracking morphologies at the nanoscale: Self-assembly of an amphiphilic designer peptide into a double helix superstructure

Show Author's information Karin Kornmueller1, Ilse Letofsky-Papst2, Kerstin Gradauer1, Christian Mikl1, Fernando Cacho-Nerin3,†, Mario Leypold4, Walter Keller5, Gerd Leitinger6,7, Heinz Amenitsch3, Ruth Prassl1( )
Institute of BiophysicsMedical University of GrazBioTechMed-Graz8010Graz, Austria
Institute for Electron Microscopy and NanoanalysisGraz University of Technology and Graz Centre for Electron Microscopy8010Graz, Austria
Institute of Inorganic ChemistryGraz University of Technology8010Graz, Austria
Institute of Organic ChemistryGraz University of Technology8010Graz, Austria
Institute for Molecular BiosciencesKarl-Franzens-University Graz8010Graz, Austria
Research Unit Electron Microscopic TechniquesInstitute of Cell BiologyHistology and EmbryologyMedical University of Graz8010Graz, Austria
Center for Medical ResearchMedical University of Graz8010Graz, Austria

† Present address: Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom

Abstract

Hierarchical self-assembly is a fundamental principle in nature, which gives rise to astonishing supramolecular architectures that are an inspiration for the development of innovative materials in nanotechnology. Here, we present the unique structure of a cone-shaped amphiphilic designer peptide. While tracking its concentration-dependent morphologies, we observed elongated bilayered single tapes at the beginning of the assembly process, which further developed into novel double-helix-like superstructures at high concentrations. This architecture is characterized by a tight intertwisting of two individual helices, resulting in a periodic pitch size over their total lengths of several hundred nanometers. Solution X-ray scattering data revealed a marked 2-layered internal organization. All these characteristics remained unaltered for the investigated period of almost three months. In their collective morphology, the assemblies are integrated into a network with hydrogel characteristics. Such a peptide-based structure holds promise as a building block for next-generation nanostructured biomaterials.

Keywords: self-assembly, TEM, spectroscopy, double helix, amphiphilic designer peptide, SAXS

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Publication history
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Acknowledgements

Publication history

Received: 18 August 2014
Revised: 05 December 2014
Accepted: 07 December 2014
Published: 28 March 2015
Issue date: June 2015

Copyright

© Tsinghua University Press and Springer-Verlag Berlin Heidelberg 2014

Acknowledgements

Acknowledgements

This work has been supported by the Austrian Science Fund (FWF Project No. I 1109-N28 to R. P.). We thank Elisabeth Bock and Gertrud Havlicek for technical assistance with electron microscopy. We gratefully acknowledge Rolf Breinbauer for providing access to infrared spectroscopy instrumentation.

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