General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides

Dathe, Margitta; Meyer, Jana; Beyermann, Michael; Maul, Björn; Hoischen, Christian; Bienert, Michael

doi:10.1016/s0005-2736(01)00429-1

Cited by 145 publications

(145 citation statements)

References 54 publications

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“…The perturbation of the lipid bilayer by specific peptide sequences is governed by a subtle equilibrium of electrostatic and hydrophobic interactions [43,44].…”

Section: Ftir Measurementsmentioning

confidence: 99%

Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

Fernández-Vidal

Rojo

Herrera

et al. 2008

Biophysical Chemistry

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Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of gbv-c/hgv virus. conformational requirements for leakage, Biophysical Chemistry (2007Chemistry ( ), doi: 10.1016Chemistry ( /j.bpc.2007 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT LIPOSOME DESTABILIZATION INDUCED BY SYNTHETIC LIPOPEPTIDES CORRESPONDING TO ENVELOPE AND NON-STRUCTURAL DOMAINS OF GBV-C/HGV VIRUS. CONFORMATIONAL REQUIREMENTS FOR LEAKAGE A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT 2 AbstractLiposomes have been used primarily as a model system for studying biological membranes.

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“…The perturbation of the lipid bilayer by specific peptide sequences is governed by a subtle equilibrium of electrostatic and hydrophobic interactions [43,44].…”

Section: Ftir Measurementsmentioning

confidence: 99%

Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

Fernández-Vidal

Rojo

Herrera

et al. 2008

Biophysical Chemistry

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“…Because antibiotic resistance develops rapidly as soon as new agents are introduced, attempts to develop antimicrobial compounds with new mechanisms of action resulted in an increased interest in the role of antimicrobial proteins and peptides (21). A wealth of information is currently available related to the mechanism of action of antimicrobial peptides (22)(23)(24). However, little is known with respect to larger polypeptides, namely, small proteins, such as ECP.…”

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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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“…The capacity of the dermaseptins to discriminate between mammalian and microbial cells has been known for more than a decade (13,14), and it is mainly due to the amino acid composition of the peptides and to the differences encountered in the physical-chemical properties of membranes (13)(14)(15)(16)(17)(18)(19)(20). Besides the phospholipid content, the cell lysis mediated by amphiphilic antimicrobial peptides such as the dermaseptins is attenuated by increasing amounts of membrane cholesterol (21,22).…”

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confidence: 99%

Dermaseptins from Phyllomedusa oreades andPhyllomedusa distincta

Brand¹,

Leite²,

Silva³

et al. 2002

Journal of Biological Chemistry

105

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Amphibian skin secretions are known as a rich source of biologically active molecules, most of which are alkaloids, biogenic amines, and peptides. Dermaseptins are a class of antimicrobial peptides present in tree frogs of the Phyllomedusa genus. They are cationic molecules of 28 -34 residues that permeabilize the membrane of Gram-positive and Gram-negative bacteria, yeasts, and filamentous fungi, showing little or no hemolytic activity. This work reports the isolation, molecular mass analysis, primary structure determination, biological activities, and potential therapeutic applications of an antimicrobial peptide found in the skin secretion of Phyllomedusa oreades, which is a newly described amphibian species endemic of the Brazilian savanna. DS 01 is a 29-residue-long peptide with a molecular mass of 2793.39 Da showing antibacterial properties against Gram-positive and Gram-negative bacteria in the range of 3-25 M. Anti-protozoan activity was investigated using T. cruzi in its trypomatigote and epimastigote forms cultivated in both cell culture and blood media. Within 2 h after incubation with DS 01 at a final concentration of ϳ6 M, no protozoan cells were detected. Two synthetic dermaseptins, described previously by our group and named dermadistinctins K and L (DD K and DD L), also had their anti-Trypanosoma cruzi activity investigated and demonstrated similar properties. Toxicity of DS 01 to mouse erythrocytes and white blood cells was evaluated by means of atomic force microscopy and flow cytometry. No morphological alterations were observed at a lytic concentration of DS 01, suggesting its therapeutic value especially as an anti-T. cruzi agent to prevent infections during blood transfusion.

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General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides

Cited by 145 publications

References 54 publications

Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

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

Dermaseptins from Phyllomedusa oreades andPhyllomedusa distincta

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