RMN et Biophysique de Membranes

The team investigates the structure-function correlations of antimicrobial peptides in membranes. In particular using oriented solid-state NMR spectroscopy we have been the first to show that cationic antimicrobial peptides such as magainins exhibit their antimicrobial action when oriented parallel to the membrane surface (rather than transmembrane helical bundles). This mechanism of action has been confirmed later with the help of designed histidine-rich peptides where the membrane topology can be controlled. More recently we have been investigating dimeric sequences such as distinctin as well as the synergistic interactions of peptides that naturally occur in cocktails stored e.g. in the frog skins. Whereas pore formation within bacterial membranes is important for the activities of antimicrobial peptides such membrane interactions are also key for the peptides to enter the cells. Therefore, it is important to realize that antimicrobial peptides can cause the agglutination of bacteria (or liposomes) as well as the compact DNA and RNA molecules. The last discovery has led us to develop some of the antimicrobial peptides into tools for nucleic acid transfection into eukaryotic cells.

Equipe «RMN et Biophysique de Membranes »

Resp. de l’équipe : Burkhard BECHINGER

Correspondant GDR : Burkhard BECHINGER, bechinge@unistra.fr

Adresse complète

1 rue Blaise Pascal

67070 Strasbourg

Code unité

UMR7177

Tutelle(s)

CNRS / Université de Strasbourg

Adresse internet du laboratoire ou institut

http://institut-chimie.unistra.fr/equipes-de-recherche/biophysique-des-membranes-et-rmn/

Lipid-interactions of the LAH4, a peptide with antimicrobial and nucleic transfection activities

Perrone, B., Miles, A.J., Salnikov, E.S., Wallace, B. and Bechinger, B. Lipid-interactions of the LAH4, a peptide with antimicrobial and nucleic transfection activities. European Biophysics Journal 43, 499-507 (201

Membrane interactions of Phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy

Resende, J.M., Verly, R.M., Aisenbrey, C., Cesar, A., Bertani, P., Piló-Veloso, D. and Bechinger, B. Membrane interactions of Phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy, Biophysical Journal 107, 901-911 (2014) doi: 10.1016/j.bpj.2014.07.014

Molecular packing of peptides at the lipid membrane surface

Aisenbrey, C. and Bechinger, B. Molecular packing of peptides at the lipid membrane surface, Langmuir 30, 10374-83 (2014) doi: 10.1021/la500998g

Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl

De Zotti, M., Ballano, G., Josta, M., Salnikov, E.S., Bechinger, B., Oance, S., Crisma, M., Toniolo, C., and Formaggio, F. Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label Chemisty and Biodiversity, 11, 1163-1191 (2014) doi: 10.1002/cbdv.201300394

Molecular Dynamics Methods to Predict Peptide Location in Membranes: LAH4 as a Stringent Test Case

Farrotti, A., Bocchinfuso, G., Palleschi, A., Rosato, N., Salnikov,E. S., Voievoda, N., Bechinger, B., Stella, L., Molecular Dynamics Methods to Predict Peptide Location in Membranes: LAH4 as a Stringent Test Case. Biochimica and Biophysica Acta, 1848, 581-592 (2015) doi: 10.1016/j.bbamem.2014.11.002

The SMART model: Soft Membranes Adapt and Respond, also Transiently, to external stimuli

Bechinger, B. The SMART model: Soft Membranes Adapt and Respond, also Transiently, to external stimuli, review, Journal of Peptide Sciences 21, 346-55 (2015) doi: 10.1002/psc.2729

A Cell Penetrating Foldamer with a Bioreducible Linkage For Intracellular Delivery of DNA

Douat, C., Aisenbrey, C., Antunes, S., Decossas, M., Lambert, O., Bechinger, B., Kichler, A. and Guichard, G. A Cell Penetrating Foldamer with a Bioreducible Linkage For Intracellular Delivery of DNA, Angewandte Chemie International Edition 54, 11133-11137 (2015) doi: 10.1002/anie.201504884

Thermodynamic and Biophysical Analysis of the Membrane-Association of a histidines-rich peptide with Efficient Antimicrobial and Transfection Activities

Voievoda, N., Schulthess, T., Bechinger, B., and Seelig, J. Thermodynamic and Biophysical Analysis of the Membrane-Association of a histidines-rich peptide with Efficient Antimicrobial and Transfection Activities »

Investigations of the synergistic enhancement of antimicrobial activity in mixtures of magainin 2 and PGLa

Glattard, E., Salnikov, E.S., Aisenbrey, C. and Bechinger, B. Investigations of the synergistic enhancement of antimicrobial activity in mixtures of magainin 2 and PGLa, Biophysical Chemistry 210, 35-44 (2016) doi: 10.1016/j.bpc.2015.06.002

Magainin 2-PGLa interactions in membranes - Two peptides that exhibit synergistic enhancement of antimicrobial activity Current Topics in Medicinal Chemistry 16

Marquette, A., Salnikov, E.S., Glattard, E., Aisenbrey, C., and Bechinger, B. Magainin 2-PGLa interactions in membranes – Two peptides that exhibit synergistic enhancement of antimicrobial activity Current Topics in Medicinal Chemistry 16, 65-75 (2016) PMID: 26139118

Molecular determinants of Vectofusin-1 and its derivatives for the enhancement of lentiviral-mediated gene transfer into hematopoietic stem/progenitor cells

Majdoul, S., Seye, A.K., Kichler, A., Holic, N., Galy, A., Bechinger, B., and Fenard, D., Molecular determinants of Vectofusin-1 and its derivatives for the enhancement of lentiviral-mediated gene transfer into hematopoietic stem/progenitor cells Journal of Biological Chemistry, 291, 2161-2169 (2016) doi: 10.1074/jbc.M115.675033

Solid-State NMR Membrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization / solid-state NMR spectroscopy

Salnikov, E. S., Aisenbrey, C., Aussenac, F., Ouari, O., Sarrouj, H., Reiter, C., Tordo, P., Engelke, F. and Bechinger, B. Solid-State NMR Membrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization / solid-state NMR spectroscopy Nature Scientific Reports 6:20895 (2016) doi: 10.1038/srep20895

Alamethicin supramolecular organization in lipid membranes from 19F solid-state NMR

Salnikov, E.S., Raya, J., De Zotti, M., Zaitseva, E., Peggion, C., Ballano, G., Toniolo, C, Rapp, J., and Bechinger, B. Alamethicin supramolecular organization in lipid membranes from 19F solid-state NMR Biophysical Journal 111, 2450-2459 (2016) doi: 10.1016/j.bpj.2016.09.048

Amphiphilicity is a key determinant in the membrane interaction of synthetic 14-mer cationic peptide analogs

Fillion, M., Goudreault, M., Voyer, N., Bechinger, B. and Auger, M. Amphiphilicity is a key determinant in the membrane interaction of synthetic 14-mer cationic peptide analogs Biochemistry 55(49), 6919-6930 (2016) DOI:10.1021/acs.biochem.6b00961

Antimicrobial Peptides – Mechanism of Action and Resistance

Bechinger, B. and Gorr, S.U. Antimicrobial Peptides – Mechanism of Action and Resistance Review, Journal of Dental Research pii: 0022034516679973. [Epub ahead of print] (2017, in press) pii: 0022034516679973. [Epub ahead of print]

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

Molay, G., Leborgne, C., Mason, A.J., Aisenbrey, C., Kichler A. and Bechinger, B. Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multiple of cargo Journal of Peptide Sciences 23, 320-328 (2017) doi: 10.1002/psc.2955

Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin

Verly, R.M., Resende, J.M., Junior, E.F.C., de Magalhães, M.T.C., Guimarães, C.F.C.R., Munhoz, V.H.O., Bemquerer, M.P., Almeida, F.C.L., Santoro, M.M., Piló-Veloso, D., and Bechinger, B. Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin. Nature Scientific Reports 7:40854, DOI: 10.1038/srep40854 (2017)

Biophysical investigations elucidating the mechanisms of action of antimicrobial peptides and their synergism

A. Marquette and B. Bechinger. Biophysical investigations elucidating the mechanisms of action of antimicrobial peptides and their synergism. Biomolecules. vol. 8, no. 2, pp. pii: E18., 2018, DOI: 10.3390/biom8020018

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

M.R. Loffredo, A. Ghosh, N. Harmouche, B. Casciaro, V. Luca, A. Bortolotti, F. Cappiello, L. Stella, A. Bhunia, B. Bechinger, and M.L. Mangoni: “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.” Biochim. Biophys. Acta – Biomembr. vol. 1859, pp. 2327–2339, 2017, DOI: 10.1016/j.bbamem.2017.09.009

Aryl-Alkyl-Lysines Interact with Anionic Lipid Components of Bacterial Cell Envelope Eliciting Anti-Inflammatory and Antibiofilm Properties

C. Ghosh, N. Harmouche, B. Bechinger, and J. Haldar: “Aryl-Alkyl-Lysines Interact with Anionic Lipid Components of Bacterial Cell Envelope Eliciting Anti-Inflammatory and Antibiofilm Properties.” ACS Omega. vol. 3, no. 8, pp. 9182–9190, 2018, DOI: 10.1021/acsomega.8b01052

The Multifaceted Antibacterial Mechanisms of the Pioneering Peptide Antibiotics Tyrocidine and Gramicidin S

M. Wenzel, M. Rautenbach, J.A. Vosloo, T. Siersma, C.H.M. Aisenbrey, E. Zaitseva, W.E. Laubscher, W. van Rensburg, J.C. Behrends, B. Bechinger, and L.W. Hamoen: “The Multifaceted Antibacterial Mechanisms of the Pioneering Peptide Antibiotics Tyrocidine and Gramicidin S.” MBio. vol. 9, pp. e00802-18, 2018, DOI: 10.1128/mbio.00802-18

Lipid-Mediated Interactions between the Antimicrobial Peptides Magainin 2 and PGLa in Bilayers

N. Harmouche and B. Bechinger: “Lipid-Mediated Interactions between the Antimicrobial Peptides Magainin 2 and PGLa in Bilayers.” Biophys. J. vol. 115, no. 6, pp. 1033–1044, 2018, DOI: 10.1016/j.bpj.2018.08.009

Tyrocidine A interactions with saccharides investigated by CD and NMR spectroscopies

D.W. Juhl, W. van Rensburg, X. Bossis, J.A. Vosloo, M. Rautenbach, and B. Bechinger: “Tyrocidine A interactions with saccharides investigated by CD and NMR spectroscopies.” J. Pept. Sci. vol. 18, pp. e3163, 2019, DOI: 10.1002/psc.3163

Solid-state NMR, membrane topology and dynamics, aggregation/agglutination, interactions in membranes, supported lipid bilayers, solution state NMR structures in micelles

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