Effect of de Novo Designed Peptides Interacting with the Lipid-Membrane Interface on the Stability of the Cubic Phases of the Monoolein Membrane

Masum, Shah Md.; Li, Shu Jie; Tamba, Yukihiro; Yamashita, Yūko; Tanaka, Tomoki; Yamazaki, Masahito

doi:10.1021/la026847l

Cited by 30 publications

(55 citation statements)

References 40 publications

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“…Therefore, it is worthy noting that in our study the presence of bilayer-forming peptide in the MO/A 6 D mixture promotes the formation of H 2 instead of the planar L α (structure with zero curvature). Different findings were reported by Yamazaki and his coworkers [62] on the effect of the positively charged peptide WLFLLKKK, which was loaded with similar concentrations, onto the MO-based Pn3m phase. This peptide with a relatively large positively charged headgroup (KKK) induces the structural transformation from V 2 (Pn3m) via V 2 (Im3m symmetry) to L α .…”

Section: Resultsmentioning

confidence: 59%

“…In a basic approach, the molecular shape can be described by the critical packing parameter (CPP) or the molecular wedge shape factor, which is defined as:where v s is the hydrophobic chain volume, a 0 is the headgroup area, and l is the hydrophobic chain length [73]. This packing parameter is controlled by various factors such as surfactant's molecular shape, temperature, hydration, the presence of hydrophilic or hydrophobic guest molecules, and electrostatic effects [16], [29]–[33], [35], [45]–[50], [61], [62].…”

Section: Resultsmentioning

confidence: 99%

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Tuning Curvature and Stability of Monoolein Bilayers by Designer Lipid-Like Peptide Surfactants

et al. 2007

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This study reports the effect of loading four different charged designer lipid-like short anionic and cationic peptide surfactants on the fully hydrated monoolein (MO)-based Pn3m phase (Q224). The studied peptide surfactants comprise seven amino acid residues, namely A6D, DA6, A6K, and KA6. D (aspartic acid) bears two negative charges, K (lysine) bears one positive charge, and A (alanine) constitutes the hydrophobic tail. To elucidate the impact of these peptide surfactants, the ternary MO/peptide/water system has been investigated using small-angle X-ray scattering (SAXS), within a certain range of peptide concentrations (R≤0.2) and temperatures (25 to 70°C). We demonstrate that the bilayer curvature and the stability are modulated by: i) the peptide/lipid molar ratio, ii) the peptide molecular structure (the degree of hydrophobicity, the type of the hydrophilic amino acid, and the headgroup location), and iii) the temperature. The anionic peptide surfactants, A6D and DA6, exhibit the strongest surface activity. At low peptide concentrations (R = 0.01), the Pn3m structure is still preserved, but its lattice increases due to the strong electrostatic repulsion between the negatively charged peptide molecules, which are incorporated into the interface. This means that the anionic peptides have the effect of enlarging the water channels and thus they serve to enhance the accommodation of positively charged water-soluble active molecules in the Pn3m phase. At higher peptide concentration (R = 0.10), the lipid bilayers are destabilized and the structural transition from the Pn3m to the inverted hexagonal phase (H2) is induced. For the cationic peptides, our study illustrates how even minor modifications, such as changing the location of the headgroup (A6K vs. KA6), affects significantly the peptide's effectiveness. Only KA6 displays a propensity to promote the formation of H2, which suggests that KA6 molecules have a higher degree of incorporation in the interface than those of A6K.

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Section: Resultsmentioning

confidence: 59%

Section: Resultsmentioning

confidence: 99%

Tuning Curvature and Stability of Monoolein Bilayers by Designer Lipid-Like Peptide Surfactants

et al. 2007

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“…15,16 As the peptide concentration increased and, thereby, the surface charge density of the MO membrane due to the bound peptide in the interface increased, the most stable phase of the MO membrane changed as follows: Q 224 w Q 229 w L R . 15,16 In biological cells, proteins and peptides may change stability of the cubic phases of biomembranes. Several peptides such as the so-called fusion peptides of membrane proteins in viruses have been reported to induce nonbilayer membranes such as the cubic phase and hexagonal (H II ) phase.…”

Section: Introductionmentioning

confidence: 99%

Effect of Positively Charged Short Peptides on Stability of Cubic Phases of Monoolein/Dioleoylphosphatidic Acid Mixtures

Masum

Awad

et al. 2005

Langmuir

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To elucidate the stability and phase transition of cubic phases of biomembranes with infinite periodic minimal surface is indispensable from biological and physicochemical aspects. In this report, we investigated the effect of positively charged peptide-3K (LLKKK) and poly(L-lysine) on the phase stability of monoolein (MO) membranes containing negatively charged dioleoylphosphatidic acid (DOPA) (i.e., DOPA/MO membranes) using small-angle X-ray scattering. At first, the effect of peptide-3K on 10% DOPA/90% MO membrane in excess water, which is in the Q229 phase, was investigated. At 3.4 mM peptide-3K, a Q229 to Q230 phase transition occurred, and at >3.4 mM peptide-3K, the membrane was in the Q230 phase. Poly(L-lysine) (M(w) 1K-4K) also induced the Q230 phase, but peptide-2K (LLKK) could not induce it in the same membrane. We also investigated the effect of peptide-3K on the multilamellar vesicle (MLV) of 25% DOPA/75% MO membrane, which is in L(alpha) phase. In the absence of peptide, the spacing of MLV was very large (11.3 nm), but at > or = 8 mM peptide-3K, it greatly decreased to a constant value (5.2 nm), irrespective of the peptide concentration, indicating that peptide-3K and the membranes form an electrostatically stabilized aggregation with low water content. Poly(L-lysine) also decreased greatly the spacing of the 25% DOPA/75% MO MLV, indicating the formation of a similar aggregation. To compare the effects of peptide-3K and poly(L-lysine) with that of osmotic stress on stability of the cubic phase, we investigated the effect of poly(ethylene glycol) with molecular weight 7500 (PEG-6K) on the phase stability of 10% DOPA/90% MO membrane. With an increase in PEG-6K concentration, i.e., with an increase in osmotic stress, the most stable phase changed as follows; Q229 (Schwartz's P surface) --> Q224 (D) --> Q230 (G). On the basis of these results, we discuss the mechanism of the effects of the positively charged short peptides (peptide-3K) and poly(L-lysine) on the structure and phase stability of DOPA/MO membranes.

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“…One family of cubic phases, which includes the Q 224 phase (space group Pn3m, Schwartz's D surface), Q 229 phase (Im3m, P surface) and Q 230 phase (Ia3d, G surface), has an infinite periodic minimal surface (IPMS) consisting of bicontinu-ous regions of water and hydrocarbon [17][18][19]. We have found that, as the concentration of peptide-1 increased, a phase transition from Q 224 to Q 229 occurred, and that, at higher peptide-1 concentrations, MO/peptide-1 membranes were in the L α phase [16]. Salts in solution inhibited these phase transitions, indicating that electrostatic interactions with adsorbed peptide-1 in the membrane interface induced these phase transitions.…”

Section: Analysis Of Shape Changes Induced In Guvs By the Interacmentioning

confidence: 95%

“…3). We have investigated the effect of peptide-1 on the stability of electrically neutral lipid membranes in the liquid-crystalline (L α ) phase [8] and in the cubic phase [16].…”

Section: Analysis Of Shape Changes Induced In Guvs By the Interacmentioning

confidence: 99%

The Single GUV Method for Probing Biomembrane Structure and Function

Yamazaki

Tamba

2005

e-J. Surf. Sci. Nanotechnol.

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Giant liposomes or giant unilamellar vesicles (GUVs) of lipid membranes, with diameter greater than 10 µm have a great advantage over smaller liposomes, e.g., large or small unilamellar vesicles, LUVs or SUVs in the investigation of biomembranes. Studies of single GUVs (the 'single GUV method') yield especially useful information on their structure and physical properties as a function of time and spatial coordinates. Here we show three examples of studies using the single GUV method: analysis of shape changes of GUVs; membrane fusion and vesicle fission; and use of a GUV as a microscopic container.

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Effect of de Novo Designed Peptides Interacting with the Lipid-Membrane Interface on the Stability of the Cubic Phases of the Monoolein Membrane

Cited by 30 publications

References 40 publications

Tuning Curvature and Stability of Monoolein Bilayers by Designer Lipid-Like Peptide Surfactants

Tuning Curvature and Stability of Monoolein Bilayers by Designer Lipid-Like Peptide Surfactants

Effect of Positively Charged Short Peptides on Stability of Cubic Phases of Monoolein/Dioleoylphosphatidic Acid Mixtures

The Single GUV Method for Probing Biomembrane Structure and Function

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