Tracking morphologies at the nanoscale: Self-assembly of an amphiphilic designer peptide into a double helix superstructure
double helix, amphiphilic designer peptide, self-assembly, SAXS, TEM, spectroscopy
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.
Tsinghua University Press
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