| Literature DB >> 26290684 |
Karin Kornmueller1, Ilse Letofsky-Papst2, Kerstin Gradauer1, Christian Mikl1, Fernando Cacho-Nerin3, Mario Leypold4, Walter Keller5, Gerd Leitinger6, Heinz Amenitsch3, Ruth Prassl1.
Abstract
Hierarchical self-assembly is a fundamental principle in nature, which gives rise to astonishing supramolecular architectures that offer an inspiration for the development of innovative materials in nanotechnology. Here we present the unique structure of a cone-shaped amphiphilic designer peptide. When 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 increased 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 for a building block of next-generation nanostructured biomaterials.Entities:
Keywords: Double helix; SAXS; TEM; amphiphilic designer peptide; self-assembly; spectroscopy
Year: 2015 PMID: 26290684 PMCID: PMC4538866 DOI: 10.1007/s12274-014-0683-9
Source DB: PubMed Journal: Nano Res ISSN: 1998-0000 Impact factor: 8.897