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Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

Nano Research 2018年第2期11卷 913-928页

作者： Karin Kornmueller Bernhard Lehofer Gerd Leitinger Heinz Amenitsch ruth prassl Institute of Biophysics Medical University of Graz BioTechMed-Graz Graz Austria Institute of Cell Biology Histology and Embryology Research Unit Electron Microscopic Techniques Medical University of Graz Graz Austria Institute of Inorganic Chemistry Graz University of Technology Graz Austria

Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as the most relevant biological representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates （V4D, V4WD, V4WD2, I4WD2） readily self-assembled into lamellae in aqueous solution. Small-angle X-ray scattering （SAXS） patterns revealed ordered lamellar structures with a repeat distance of 4-5 nm. Transmission electron microscopy （TEM） images confirmed the presence of stacked sheets. Two derivatives （V3D and V4D2） remained as loose aggregates dispersed in solution; one peptide （L4WD2） formed twisted tapes with internal lameUae and an antiparaUel -type monomer aligrtment. To understand the interaction of peptides with lipids, they were mixed with phosphatidylcholines. Low peptide concentrations （1.1 mM） induced the formation of a heterogeneous mixture of vesicular structures. Large multilamellar vesicles （MLV, d-spacing - 6.3 nm） coexisted with oligo- or unilamellar vesicles （- 50 nm in diameter） and bicelle-like structures （- 45 nm length, - 18 nm width）. High peptide concentrations （11 mM） led to unilamellar vesicles （ULV, diameter - 260-280 nm） with a homogeneous mixing of lipids and peptides. SAXS revealed the temperature-dependent fine structure of these ULVs. At 25 ℃ the bilayer is in a fully Interdigitated state （headgroup-to-headgroup distance dH, -2.9 nm）, whereas at 50 ℃this interdigitation opens up （dtm- 3.6 nm）. Our results highlight the versatility of self-assembled peptide superstructures. Subtle changes in the amino acid composition are key design elements in creating peptide- or lipid- peptide nanostructures with richness in morphology similar to that of naturally occurrin~ lioids.

关键词： amphiphilic designerpeptides lipids nanostructures lamellae small-angle X-rayscattering (SAXS) transmission electronmicroscopy (TEM)

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

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Nano Research 2015年第6期8卷 1822-1833页

作者： Karin Kornmueller Ilse Letofsky-Papst Kerstin Gradauer Christian Mikl Fernando Cacho-Nerin Mario Leypold Walter Keller Gerd Leitinger Heinz Amenitsch ruth prassl Institute of Biophysics Medical University ofGraz BioTechMed-Graz 8010 Graz Austria Institute for Electron Microscopy and Nanoanalysis Graz University of Technology and Graz Centre for Electron Microscopy 80 10 Graz A us tria Institute of Inorganic Chemistry Graz University of Technology 8010 Graz Austria Institute of Organic Chemistry Graz University of Technology 8010 Graz Austria Institute for Molecular Biosciences KarI-Franzens-University Graz 8010 Graz Austria Research Unit Electron Microscopic Techniques Institute of Cell Biology Histology and Embryology Medical University of Graz 80 10 Graz A us tria Center for Medical Research Medical University of Graz 8010 Graz Austria

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 nanotechnolog）a 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.

关键词： double helix amphiphilic designerpeptide self-assembl)~SAXS TEM spectroscopy

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