extlogo-cbmnlogo-iecb

Resp. Erick Dufourc (This email address is being protected from spambots. You need JavaScript enabled to view it., Tel: +33 5 40 00 68 18)
Corr. Axelle Grélard ( This email address is being protected from spambots. You need JavaScript enabled to view it. , Tel: +33 5 40 00 22 30)

 pano

Institute of Chemistry & Biology of Membranes & Nano-objects /  European Institut of Chemistry and Biology

Platform Technical Description:

Spectrometer 800 MHz for applications in Liquid, Solid & Soft matter

Console:
Bruker Avance III, 4 channels

Work Station:
Environnement Linux, software Topspin 3.1

NMR Probes:
Cryoprobe 5mm TCI 1H-13C/15N/2H with Z-gradient, (S/B =x), T= 4-50 °C
CPMAS 4 mm probe 2 channels: 1H/BB
CPMAS 3.2 mm probe 3 channels: 1H/13C/15N

photoNMR experiments available:

Liquid state NMR experiments (all multidimensional experiemnts including those in weakly oriented media).

Soft matter NMR: membranes, colloids or liquid crystals. Wide line, magic angle sample spinning and oriented samples.

Solid state NMR experiments (CPMAS) including fibrilar or microcrystalline proteins

Main domains of interest:

  • NMR of membrane lipids in the context of bicelles, liposomes, membrane domains "rafts", atherosclerosis & cellular signaling (nanoobjets orineted by magnetic fields, sterols, phosphoinositides, etc.)
  • NMR of membrane peptides and proteins involved in cancer, apoptosis or with antimicrobial or antibiotic properties (neu/erbB-2, Bax, Bcl-2, Melittin, Surfactin, Cateslytin, etc.)
  • NMR of natural colloids in health and nutrition domains (tannins/saliva proteins, sprayable lipoaminoacids/active proteins).
  • CP MAS NMR of fibrilar proteins involved in supramolacular complexes.
  • Supramolecular and bioorganic chemistry, foldamers and peptidomimetics
  • Self assembly of amphilphilic molecules
  • Synthesis & Acrivity of natural substances of biological interest  (phenols & quinones)
  • 3D structure of nucleic acids, proteins and their complexes
  • Solid state Chemistry, materials, alloys.
  • 2D-3D multinuclear liquid state NMR
  • RDC (residual dipolar coupling)
  • Relaxation13C15N2H31P

 

Other NMR Equipments on the platform:

700 MHz Bruker Avance NEO Liquids / Solids

LS NMR Probes:
TXI (1H, 13C, 15N, 2H), 5 mm, z-gradients
BBO (109Ag – 31P, 1H, 2H), 5 mm, z-gradients
HRMAS (1H, 13C, 15N, 2H), 4 mm
SS NMR Probes:
CPMAS (1H, 2H, 31P), 4 mm, E-free
CPMAS (15N – 31P, 1H), 4 mm

600 MHz Bruker Avance NEO Solids

SS NMR Probes:
CPMAS (1H, 13C, 15N), 4 mm, E-free
CPMAS (1H, 13C, 15N), 3.2 mm, E-free
CPMAS (1H, 13C, 15N, 2H), 1.3 mm, E-free
CPMAS (1H, X), 4mm

500 MHz Bruker Avance III  Solids

SS NMR Probes:
CPMAS (1H, X), for low-gamma nuclei, 4 mm
CPMAS (1H, X, Y), 2,5 mm
CPMAS (1H, X), 4 mm

400 MHz Bruker Avance III-HD Liquids

LS NMR Probes:
Smart-Probe (X-19F, 1H, 2H), 5 mm, z-gradients
QNP (13C-31P-19F, 1H, 2H), 5 mm, z-gradients
BBI (15N-31P, 1H, 2H), 5 mm, z-gradients

300 MHz Bruker Avance I Solids

SS NMR Probes:
CPMAS (1H, X, Y), 4 mm
CPMAS (1H, X, Y), 4 mm, high temperatures (< 300°C)
WL Gonio automatic (1H, X, Y), rotors de 4 ou 7 mm

300 MHz Bruker Avance II Liquids

LS NMR Probe:
BBFO (15N-31P, 1H, 2H), 5 mm, z-gradients

100 MHz Bruker Avance II Solids

SS NMR Probe:
MAS (X, Y), 4 mm

A propos : CBMN & IECB

The institute of Chemistry and Biology of Membranes and Nano-objects (CBMN) is an institute belonging to CNRS, University of Bordeaux and to the Bordeaux Polytechnic Institute. It is multi-disciplinary and operates at the interface between Chemistry, Biology and Physics by hosting 14 research laboratories distributed in three departments: Biomimetic and Therapeutic Chemistry, Biophysical Chemistry and Biology and Biotechnology. 8 Technical Platforms (NMR, X-Rays, Electron Microscopy, Mass spectrometry, Vibrational spectroscopy (IR-Raman-BA-PWR), Molecular Modelling, AFM, and peptide synthesis.) nicely complement the high level expertise of research laboratories. CBMN is part a national plan called “Invest to the Future”: IDEX Bordeaux, Labex AMADEUS, VIBNANO and LISA Carnot Institute. A close partnership is particularly developed with pharmaceutical and formulation industries and also with industries in the nutrition and health domains (lipids and vine/wine products).

The European Institute for Chemistry & Biology (IECB), UMS 3033, is an incubator of international and interdisciplinary research teams at the interface between chemistry and biology. The platform of structural  biophysical chemistry gathers several equipments and expertises available at IECB to answer structural and functionnal questions on molecules of medical interest, with particular emphasis on topics related to biomembranes, supramolecular chemistry and gene transfer.

 

Coming to CBMN/IECB:

 

Some recent publications:

1.          Amrane, S., Rebora, K., Zniber, I., Dupuy, D., and Mackereth, C. D. (2014) Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition. Nature Communications 5

2.           Berthelot, K., Lecomte, S., Estevez, Y., Zhendre, V., Henry, S., Thevenot, J., Dufourc, E. J., Alves, I. D., and Peruch, F. (2014) Rubber particle proteins, HbREF and HbSRPP, show different interactions with model membranes. Biochimica et biophysica acta 1838, 287-299

3.          Cala, O., Dufourc, E. J., Fouquet, E., Manigand, C., Laguerre, M., and Pianet, I. (2012) The Colloidal State of Tannins Impacts the Nature of Their Interaction with Proteins: The Case of Salivary Proline-Rich Protein/Procyanidins Binding. Langmuir 28, 17410-17418

4.          Chandramouli, N., Ferrand, Y., Lautrette, G., Kauffmann, B., MacKereth, C. D., Laguerre, M., Dubreuil, D., and Huc, I. (2015) Iterative design of a helically folded aromatic oligoamide sequence for the selective encapsulation of fructose. Nature Chemistry 7, 334-341

5.          Chevelkov, V., Habenstein, B., Loquet, A., Giller, K., Becker, S., and Lange, A. (2014) Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins. Journal of Magnetic Resonance 242, 180-188

6.          Collie, G. W., Pulka-Ziach, K., Lombardo, C. M., Fremaux, J., Rosu, F., Decossas, M., Mauran, L., Lambert, O., Gabelica, V., Mackereth, C. D., and Guichard, G. (2015) Shaping quaternary assemblies of water-soluble non-peptide helical foldamers by sequence manipulation. Nature Chemistry 7, 871-878

7.          Daskalov, A., Habenstein, B., Martinez, D., Debets, A. J. M., Sabaté, R., Loquet, A., and Saupe, S. J. (2015) Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold. PLoS Biology 13

8.          Demers, J. P., Habenstein, B., Loquet, A., Kumar Vasa, S., Giller, K., Becker, S., Baker, D., Lange, A., and Sgourakis, N. G. (2014) High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy. Nature Communications 5

9.          Douat, C., Aisenbrey, C., Antunes, S., Decossas, M., Lambert, O., Bechinger, B., Kichler, A., and Guichard, G. (2015) A Cell-Penetrating Foldamer with a Bioreducible Linkage for Intracellular Delivery of DNA. Angewandte Chemie - International Edition

10.        Douliez, J. P., Zhendre, V., Grélard, A., and Dufourc, E. J. (2014) Aminosilane/oleic acid vesicles as model membranes of protocells. Langmuir 30, 14717-14724

11.        Fremaux, J., Mauran, L., Pulka-Ziach, K., Kauffmann, B., Odaert, B., and Guichard, G. (2015) α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers. Angewandte Chemie - International Edition 54, 9816-9820

12.        Furlan, A. L., Jobin, M. L., Pianet, I., Dufourc, E. J., and Géan, J. (2015) Flavanol/lipid interaction: A novel molecular perspective in the description of wine astringency & bitterness and antioxidant action. Tetrahedron 71, 3143-3147

13.        Habenstein, B., and Loquet, A. (2015) Solid-state NMR: An emerging technique in structural biology of self-assemblies. Biophysical Chemistry

14.        Habenstein, B., Loquet, A., Hwang, S., Giller, K., Vasa, S. K., Becker, S., Habeck, M., and Lange, A. (2015) Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli. Angewandte Chemie - International Edition

15.        Mendoza, O., Porrini, M., Salgado, G. F., Gabelica, V., and Mergny, J. L. (2015) Orienting tetramolecular G-quadruplex formation: The quest for the elusive rna antiparallel quadruplex. Chem. Eur. J. 21, 6732-6739

16.          Pulka-Ziach, K., Pavet, V., Chekkat, N., Estieu-Gionnet, K., Rohac, R., Lechner, M. C., Smulski, C. R., Zeder-Lutz, G., Altschuh, D., Gronemeyer, H., Fournel, S., Odaert, B., and Guichard, G. (2015) Thioether analogues of disulfide-bridged cyclic peptides targeting death receptor 5: Conformational analysis, dimerisation and consequences for receptor activation. ChemBioChem 16, 293-301

17.          Salgado, G. F., Cazenave, C., Kerkour, A., and Mergny, J.-L. (2015) G-quadruplex DNA and ligand interaction in living cells using NMR spectroscopy. Chemical Science 6, 3314-3320

18.          Uzureau, P., Uzureau, S., Lecordier, L., Fontaine, F., Tebabi, P., Homble, F., Grelard, A., Zhendre, V., Nolan, D. P., Lins, L., Crowet, J.-M., Pays, A., Felu, C., Poelvoorde, P., Vanhollebeke, B., Moestrup, S. K., Lyngso, J., Pedersen, J. S., Mottram, J. C., Dufourc, E. J., Perez-Morga, D., and Pays, E. (2013) Mechanism of Trypanosoma brucei gambiense resistance to human serum. Nature 501, 430-+

19.          Vasa, S., Lin, L., Shi, C., Habenstein, B., Riedel, D., Kühn, J., Thanbichler, M., and Lange, A. (2015) β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America 112, E127-E136

 

 

Some 2013 “Highligths”, for which the TGIR RMN THC Bordeaux platform has been used (in french):

Pourquoi les parasites responsables de la maladie du sommeil résistent à la défense immunitaire de l'homme?

Le Yin et le Yang des virus : l’enveloppe de la particule antigénique à la base du vaccin contre l’hépatite B est à la fois fluide et résistante à la lyophilisation