Nano Research

, Volume 11, Issue 2, pp 913–928 | Cite as

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

  • Karin Kornmueller
  • Bernhard Lehofer
  • Gerd Leitinger
  • Heinz Amenitsch
  • Ruth PrasslEmail author
Open Access
Research Article


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 lamellae and an antiparallel β-type monomer alignment. 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 °C the bilayer is in a fully interdigitated state (headgroup-to-headgroup distance dHH ∼ 2.9 nm), whereas at 50 °C this interdigitation opens up (dHH ∼ 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 lipidpeptide nanostructures with richness in morphology similar to that of naturally occurring lipids.


amphiphilic designer peptides lipids nanostructures lamellae small-angle X-ray scattering (SAXS) transmission electron microscopy (TEM) 



This work has been supported by the Austrian Science Fund (FWF Project No. I 1109-N28 to R. P.). We gratefully acknowledge Elisabeth Pritz for her support and technical guidance with electron microscopy. We thank Hanna Lindermuth and Hans Krebs for technical assistance.

Supplementary material

12274_2017_1702_MOESM1_ESM.pdf (1.4 mb)
Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures


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Open Access: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

Authors and Affiliations

  • Karin Kornmueller
    • 1
  • Bernhard Lehofer
    • 1
  • Gerd Leitinger
    • 2
  • Heinz Amenitsch
    • 3
  • Ruth Prassl
    • 1
    Email author
  1. 1.Institute of BiophysicsMedical University of Graz, BioTechMed-GrazGrazAustria
  2. 2.Institute of Cell Biology, Histology and Embryology, Research Unit Electron Microscopic TechniquesMedical University of GrazGrazAustria
  3. 3.Institute of Inorganic ChemistryGraz University of TechnologyGrazAustria

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