Article Title

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

Authors

Karin Kornmueller, Institute of Biophysics, Medical University of Graz, BioTechMed-Graz, 8010 Graz, Austria
Ilse Letofsky-Papst, Institute for Electron Microscopy and Nanoanalysis, Graz University of Technology and Graz Centre for Electron Microscopy, 8010 Graz, Austria
Kerstin Gradauer, Institute of Biophysics, Medical University of Graz, BioTechMed-Graz, 8010 Graz, Austria
Christian Mikl, Institute of Biophysics, Medical University of Graz, BioTechMed-Graz, 8010 Graz, Austria
Fernando Cacho-Nerin, Institute of Inorganic Chemistry, Graz University of Technology, 8010 Graz, Austria
Mario Leypold, Institute of Organic Chemistry, Graz University of Technology, 8010 Graz, Austria
Walter Keller, Institute for Molecular Biosciences, Karl-Franzens-University Graz, 8010 Graz, Austria
Gerd Leitinger, Research Unit Electron Microscopic Techniques, Institute of Cell Biology, Histology and Embryology, Medical University of Graz, 8010 Graz, Austria Center for Medical Research, Medical University of Graz, 8010 Graz, Austria
Heinz Amenitsch, Institute of Inorganic Chemistry, Graz University of Technology, 8010 Graz, Austria
Ruth Prassl, Institute of Biophysics, Medical University of Graz, BioTechMed-Graz, 8010 Graz, Austria

Keywords

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

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.

Graphical Abstract

DOI

https://doi.org/10.1007/s12274-014-0683-9

Publisher

Tsinghua University Press

Recommended Citation

Karin Kornmueller,Ilse Letofsky-Papst,Kerstin Gradauer,Christian Mikl,Fernando Cacho-Nerin,Mario Leypold,Walter Keller,Gerd Leitinger,Heinz Amenitsch,Ruth Prassl, Tracking morphologies at the nanoscale: Self-assembly of an amphiphilic designer peptide into a double helix superstructure. NanoRes.2015, 8(6): 1822–1833