Membrane Biophysics and NMR

Publications 2017

Vectofusin-1, a potent peptidic enhancer of viral gene transfer forms pH-dependent α-helical nanofibrils, concentrating viral particles.

Vermeer LS, Hamon L, Schirer A, Schoup M, Cosette J, Majdoul S, Pastré D, Stockholm D, Holic N, Hellwig P, Galy A, Fenard D, Bechinger B.

Acta Biomater. 2017 Dec;64:259-268. doi: 10.1016/j.actbio.2017.10.009.

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Membrane perturbing activities and structural properties of the frog-skin derived peptide Esculentin-1a(1-21)NH2 and its Diastereomer Esc(1-21)-1c: Correlation with their antipseudomonal and cytotoxic activity.

Loffredo MR, Ghosh A, Harmouche N, Casciaro B, Luca V, Bortolotti A, Cappiello F, Stella L, Bhunia A, Bechinger B, Mangoni ML.

Biochim Biophys Acta. 2017 Dec;1859(12):2327-2339. doi: 10.1016/j.bbamem.2017.09.009.

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The histidine-rich peptide LAH4-L1 strongly promotes PAMAM-mediated transfection at low nitrogen to phosphorus ratios in the presence of serum.

Liu N, Bechinger B, Suss R.

Sci Rep. 2017 Aug 29;7(1):9585. doi: 10.1038/s41598-017-10049-y.

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pH-Dependent Membrane Interactions of the Histidine-Rich Cell-Penetrating Peptide LAH4-L1.

olf J, Aisenbrey C, Harmouche N, Raya J, Bertani P, Voievoda N, Süss R, Bechinger B.

Biophys J. 2017. pii: S0006-3495(17)30736-1. doi: 10.1016/j.bpj.2017.06.053.

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Solution and Solid-State Nuclear Magnetic Resonance Structural Investigations of the Antimicrobial Designer Peptide GL13K in Membranes.

Harmouche N, Aisenbrey C, Porcelli F, Xia Y, Nelson SED, Chen X, Raya J, Vermeer L, Aparicio C, Veglia G, Gorr SU, Bechinger B.

Biochemistry. 2017. doi: 10.1021/acs.biochem.7b00526.

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Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples.

Salnikov ES, Abel S, Karthikeyan G, Karoui H, Aussenac F, Tordo P, Bechinger B, Ouari O.

Chemphyschem. 2017;18(15):2103-2113. doi: 10.1002/cphc.201700389.

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Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin.

Verly RM, Resende JM, Junior EF, de Magalhaes MT, Guimaraes CF, Munhoz VH, Bemquerer MP, Almeida FC, Santoro MM, Pilo-Veloso D, Bechinger B.

Sci Rep. 2017;7:40854. doi: 10.1038/srep40854.

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Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multitude of cargo.

Moulay G, Leborgne C, Mason AJ, Aisenbrey C, Kichler A, Bechinger B.

J Pept Sci.;23(4):320-328. doi: 10.1002/psc.2955.

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Antimicrobial Peptides: Mechanisms of Action and Resistance.

Bechinger B, Gorr SU.

J Dent Res. 2017;96(3):254-260. doi: 10.1177/0022034516679973.

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Membrane Biophysics and NMR

Publications 2017

Vectofusin-1, a potent peptidic enhancer of viral gene transfer forms pH-dependent α-helical nanofibrils, concentrating viral particles.

Membrane perturbing activities and structural properties of the frog-skin derived peptide Esculentin-1a(1-21)NH2 and its Diastereomer Esc(1-21)-1c: Correlation with their antipseudomonal and cytotoxic activity.

The histidine-rich peptide LAH4-L1 strongly promotes PAMAM-mediated transfection at low nitrogen to phosphorus ratios in the presence of serum.

pH-Dependent Membrane Interactions of the Histidine-Rich Cell-Penetrating Peptide LAH4-L1.

Solution and Solid-State Nuclear Magnetic Resonance Structural Investigations of the Antimicrobial Designer Peptide GL13K in Membranes.

Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples.

Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin.

Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multitude of cargo.

Antimicrobial Peptides: Mechanisms of Action and Resistance.

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