Self‐assembling amphiphilic peptides

Dehsorkhi, Ashkan; Castelletto, Valeria; Hamley, Ian W.

doi:10.1002/psc.2633

Cited by 333 publications

(297 citation statements)

References 178 publications

(345 reference statements)

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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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Section: Introductionmentioning

confidence: 99%

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

et al. 2017

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“…Some of their potential uses include drug delivery, tissue engineering and antimicrobial agents. 1 The self-assembly of PAs and peptide-based molecules can be tuned by control of pH, temperature, concentration and other factors, as discussed in other reviews. 1,8,[16][17][18] This gives excellent scope to create biomaterials responsive to many or multiple environmental cues.…”

Section: Peptide Amphiphiles (Pas)mentioning

confidence: 99%

“…7 These non-covalent interactions include van der Waals forces, hydrophobic interactions, electrostatic interactions, hydrogen bonding and π-π stacking (aromatic) interactions. 1,8 These interactions are weak, for example the backbone hydrogen bonding in peptides having an estimated energy of 4.2 kcal mol −1 in a gaseous environment, which decreases in solution. 9 However, these interactions are enough to stabilise these robust structures.…”

Section: Peptide Self-assemblymentioning

confidence: 99%

“…1 This occurs through a bottom-up approach. Most self-assembling molecules have both hydrophobic and hydrophilic components, and are termed amphiphilic.…”

Section: Peptide Self-assemblymentioning

confidence: 99%

“…Most self-assembling molecules have both hydrophobic and hydrophilic components, and are termed amphiphilic. 1 Lipids are perhaps the simplest molecule displaying amphiphilicity, with a hydrophilic head group, and a hydrophobic tail group. Peptides and proteins are more complex in their amphiphilicity.…”

Section: Peptide Self-assemblymentioning

confidence: 99%

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Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

2017

Self Cite

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Molecular self-assembly is a multi-disciplinary field of research, with potential chemical and biological applications. One of the main driving forces of self-assembly is molecular amphiphilicity, which can drive formation of complex and stable nanostructures. Self-assembling peptide and peptide conjugates have attracted great attention due to their biocompatibility, biodegradability and biofunctionality. Understanding assembly enables the better design of peptide amphiphiles which may form useful and functional nanostructures. This review covers self-assembly of amphiphilic peptides and peptide mimetic materials, as well as their potential applications. Peptide self-assemblySelf-assembly is defined as the ability of a molecule, without guidance of external factors, to associate through non-covalent interactions to form highly ordered 3-dimensional structures.

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Programming Micelles with Biomolecules

Thompson

Gianneschi

2018

Self‐Assembly

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Self‐assembling amphiphilic peptides

Cited by 333 publications

References 178 publications

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

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

Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

Programming Micelles with Biomolecules

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