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

Kornmueller, Karin; Letofsky-Papst, Ilse; Gradauer, Kerstin; Mikl, Christian; Cacho-Nerin, Fernando; Leypold, Mario; Keller, Walter; Leitinger, Gerd; Amenitsch, Heinz; Ruth, Peter

doi:10.1007/s12274-014-0683-9

Cited by 22 publications

(24 citation statements)

References 51 publications

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“…11d). Similar spectra have been attributed to β-sheet or β-turn structures in very short peptides that self-assemble into supramolecular nanofibres606162. Finally, ThT binding was well consistent with the presence of β-sheets (Supplementary Fig.…”

Section: Resultssupporting

confidence: 74%

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

et al. 2016

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Mimicking the multifunctional bacterial type IV pili (T4Ps) nanofibres provides an important avenue towards the development of new functional nanostructured biomaterials. Yet, the development of T4Ps-based applications is limited by the inability to form these nanofibres in vitro from their pilin monomers. Here, to overcome this limitation, we followed a reductionist approach and designed a self-assembling pilin-based 20-mer peptide, derived from the presumably bioelectronic pilin of Geobacter sulfurreducens. The designed 20-mer, which spans sequences from both the polymerization domain and the functionality region of the pilin, self-assembled into ordered nanofibres. Investigation of the 20-mer revealed that shorter sequences which correspond to the polymerization domain form a supramolecular β-sheet, contrary to their helical configuration in the native T4P core, due to alternative molecular recognition. In contrast, the sequence derived from the functionality region maintains a native-like, helical conformation. This study presents a new family of self-assembling peptides which form T4P-like nanostructures.

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Section: Resultssupporting

confidence: 74%

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

et al. 2016

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“…While formation of the 1D nanowire is already quite challenging, coiling or twisting them into double helix can be much more difficult. Besides those structures assembled with chiral molecules like the DNA molecules or using them as templates, there are only a few cases of double helical nanowires. Physical confinement can sometimes induce formation of helical or double helix, and external shear/twist force works for certain polymeric materials as well as carbon nanotubes .…”

Section: Comparisons Between the Two Systems Of Double‐helix Formationmentioning

confidence: 99%

Twisting Ultrathin Au Nanowires into Double Helices

Lü

Yang

et al. 2018

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Previously, double helix nanowire was reported by coating Pd/Pt/Au onto Au-Ag alloy nanowire. Here, straight oleylamine-stabilized ultrathin Au nanowires with single crystalline fcc lattice are surprisingly converted into double helix helices upon reacting with Ag in tetrahydrofuran (THF). The obtained Au-Ag helical nanowires contain lattice distinctively different from the fcc lattice and are different in many aspects with the previous system. The discovery may expand the scope of nanoscale double helix formation and the understanding of lattice transformation among ultrafine nanostructures.

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“…Above a critical aggregation concentration (CAC), amphiphiles selfassemble into supramolecular structures similar to lipid mesophases. Several one-dimensional (1D) and two-dimensional (2D) structures have been reported, including micelles, cylinders, and lamellar or hexagonal phases [6][7][8][9][10][11][12][13][14][15][16][17]. Not only do peptides structurally resemble lipid molecules, but they also exhibit similar surfactant-like properties.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2017

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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 (V 4 D, V 4 WD, V 4 WD 2 , I 4 WD 2 ) 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 (V 3 D and V 4 D 2 ) remained as loose aggregates dispersed in solution; one peptide (L 4 WD 2 ) 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 d HH ~ 2.9 nm), whereas at 50 °C this interdigitation opens up (d HH ~ 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.

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

Cited by 22 publications

References 51 publications

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

Twisting Ultrathin Au Nanowires into Double Helices

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

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