Interactions of basic amphiphilic peptides with dimyristoylphosphatidylcholine small unilamellar vesicles: Optical, NMR, and electron microscopy studies and conformational calculations

Reynaud, J.A.; Grivet, Jean‐Philippe; Sy, D.; Trudelle, Y.

doi:10.1021/bi00070a005

Cited by 46 publications

(28 citation statements)

References 50 publications

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“…The high amphiphilicity of the solution structure of PGAa in membrane mimicking environments strongly suggests that PGAa peptide is capable of inactivating several pathogenic bacteria by the pore formation, as shown previously (7,29,30). The tertiary structures of PGAa determined by NMR spectroscopy shows that all of the hydrophobic side chains protrude toward one side, while the positively charged side chains protrude toward the other side as shown in Figs.…”

Section: Biological Implication Of Pgaa Structuressupporting

confidence: 69%

Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Hong

Jeong

Jung

et al. 2000

Biochemical and Biophysical Research Communications

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Section: Biological Implication Of Pgaa Structuressupporting

confidence: 69%

Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Hong

Jeong

Jung

et al. 2000

Biochemical and Biophysical Research Communications

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“…As we show, NPY interacts particularly strongly with anionic lipids, and this may induce sorting of lipids in-plane such that anionic lipids would be sequestered to the surfacebound peptide. 42 The results for charged monolayers presented in Fig. 4 then suggest that the local interaction may induce a state in which the peptide is in the transition regime between loosely associated with the surface and embedded within the lipid headgroups.…”

Section: Discussionmentioning

confidence: 83%

Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies

Dyck

Lösche

2006

J. Phys. Chem. B

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The association of neuropeptide Y (NPY) with air/water interfaces and with phospholipid monolayers on water subphases and on physiological buffer has been investigated. Surface pressure (π) vs. molecular area (A) relations of the peptide at water surfaces depend on the concentration of the spreading solutions. Independent of that concentration, they show a transition from a low-density state to a high-density state at π ∼ 12 mN/m. Similar features are observed in the NPY adsorption to preformed monolayers (Δπ(t→∞) as a function of π i = π(t=0) where t = 0 signifies the time of peptide injection). The transition is also observed in cospread lipid/NPY monolayers and is interpreted as the exclusion of the peptide from the surface layer. The reproducibility of the isotherms after expansion suggests that cospread lipid/peptide monolayers are thermodynamically stable and that the peptide remains associated with the monolayer after exclusion from the lipid surface.A comparison of NPY association with zwitterionic and with anionic lipids, as well as a comparison of the interactions on pure water and on physiological buffer, suggests that electrostatic attraction plays a major role in the energetics of peptide binding to the membrane surface. Dual label fluorescence microscopy demonstrates that the peptide associates preferentially with the disordered liquid-condensed (LC) monolayer phase and also suggests that it self-aggregates upon exceeding a critical surface concentration. A NPY variant with a distorted α-helix interacts with the surface as strongly as the natural NPY but expands the monolayers more. This suggests that the helix motif in the peptide is more important for the interaction with the receptor than for binding of the peptide to the membrane surface. In context, these observations attribute a specific role to the membrane in funneling the signal peptide to its membrane receptor.

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“…The main target of antimicrobial peptides is the bacteria inner membrane, with a net negative charge (25,56,57). The interaction of the protein with the membrane would involve both hydrophobic interactions with the lipid acyl chain and electrostatic interactions between the positive residues and anionic phospholipid head groups (58,59).…”

Section: Discussionmentioning

confidence: 99%

Topography Studies on the Membrane Interaction Mechanism of the Eosinophil Cationic Protein

et al. 2006

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The eosinophil cationic protein (ECP) is an antipathogen protein involved in the host defense system. ECP displays bactericidal and membrane lytic capacities [Carreras et al. (2003) Biochemistry 42, 6636-6644]. We have now characterized in detail the protein-membrane interaction process. All observed fluorescent parameters of the wild type and single-tryptophan-containing mutants, as well as the results of decomposition analysis of protein fluorescence, suggest that W10 and W35 belong to two distinct spectral classes I and III, respectively. Tryptophan residues were classified and assigned to distinct structural classes using statistical approaches based on the analysis of tryptophan microenvironment structural properties. W10 belongs to class I and is buried in a relative nonpolar, nonflexible protein environment, while W35 (class III) is fully exposed to free water molecules. Tryptophan solvent exposure and the depth of the protein insertion in the lipid bilayer were monitored by the degree of protein fluorescence quenching by KI and brominated phospholipids, respectively. Results indicate that W35 partially inserts into the lipid bilayer, whereas W10 does not. Further analysis by electron microscopy and dynamic light scattering indicates that ECP can destabilize and trigger lipid vesicle aggregation at a nanomolar concentration range, corresponding to about 1:1000 protein/lipid ratio. No significant leakage of the vesicle aqueous content takes place below that protein concentration threshold. The data are consistent with a membrane destabilization "carpet-like" mechanism.

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Interactions of basic amphiphilic peptides with dimyristoylphosphatidylcholine small unilamellar vesicles: Optical, NMR, and electron microscopy studies and conformational calculations

Cited by 46 publications

References 50 publications

Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Solution Structure of a Designed Amphipathic Antimicrobial Synthetic Peptide, PGAa

Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies

Topography Studies on the Membrane Interaction Mechanism of the Eosinophil Cationic Protein

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