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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Kornmueller, K; Letofsky-Papst, I; Gradauer, K; Mikl, C; Cacho-Nerin, F; Leypold, M; Keller, W; Leitinger, G; Amenitsch, H; Prassl, R.
Tracking morphologies at the nanoscale: self-assembly of an amphiphilic designer peptide into a double helix superstructure.
Nano Res. 2015; 8(6):1822-1833 Doi: 10.1007/s12274-014-0683-9 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG

 

Führende Autor*innen der Med Uni Graz
Kornmüller Karin
Prassl Ruth
Co-Autor*innen der Med Uni Graz
Leitinger Gerd
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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.

Find related publications in this database (Keywords)
double helix
amphiphilic designer peptide
self-assembly
SAXS
TEM
spectroscopy
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