RMN : Nuclear Magnetic Resonance
UMR8576 – CNRS – Lille University – Institut Pasteur de Lille
The NMR laboratory is a technical platform of the Institut Pasteur de Lille. The laboratory is equipped with a 600MHz spectrometer with cryo-probe and sample changer, as well as a 300MHz spectrometer equipped with a sample changer.
The 300MHz low-field spectrometer is dedicated to the analytical control of small molecules to allow a fine analytical characterization of synthesized compounds or isolated natural products. Users can access it after having received training in its use.
The data obtained from the 600MHz spectrometer consolidates various research projects by allowing :
- Screening of ligand-protein target interactions for medicinal chemistry
- The structural characterization of peptides and small proteins
- The study of protein-protein interactions
This equipment is also used to develop new acquisition methods (Non Uniform Sampling, homodecoupling) to reduce measurement time and facilitate spectral analyzes of compounds.
The technical platform welcomes academic and industrial users.
CPER CTRL Longevity allowed the installation of sample changers and consoles of the latest generation on both the 300 and 600 MHz spectrometers, allowing optimal use of all the functionalities. In particular, we observed fluorine nucleus with high sensitivity, an essential element in current and future screening processes for molecules of therapeutic interest. This possibility is only offered for a very limited number of academic sites in France.
ANR 2018-2022 Partner X. Hanoulle, Coordinator N. Willand.
European Innovative Training Network 2016-2020 Partner I. Landrieu, Coordinator C. Ottmann, Tue Eindhoven, Pays-Bas.
2012-2020, 2020-2025 Partner I. Landrieu, Coordinator P. Amouyel.
DR, CNRS, responsable scientifique
IR, Univ Lille, responsable technique
Faïon L, Djaout K, Frita R, Pintiala C, Cantrelle FX, Moune M, Vandeputte A, Bourbiaux K, Piveteau C, Herledan A, Biela A, Leroux F, Kremer L, Blaise M, Tanina A, Wintjens R, Hanoulle X, Déprez B, Willand N, Baulard AR, Flipo M.
Discovery of the first Mycobacterium tuberculosis MabA (FabG1) inhibitors through a fragment-based screening.
Eur J Med Chem. 2020; 200:112440. doi: 10.1016/j.ejmech.2020.112440.
Valenti D, Neves JF, Cantrelle FX, Hristeva S, Lentini Santo D, Obšil T, Hanoulle X, Levy LM, Tzalis D, Landrieu I, Ottmann C.
Set-up and screening of a fragment library targeting the 14-3-3 protein interface.
Medchemcomm. 2019; 10:1796-1802. doi: 10.1039/c9md00215d.
Kuusk A, Neves JF, Bravo-Rodriguez K, Gunnarsson A, Ruiz-Blanco YB, Ehrmann M, Chen H, Landrieu I, Sanchez-Garcia E, Boyd H, Ottmann C, Doveston RG.
Adoption of a Turn Conformation Drives the Binding Affinity of p53 C-Terminal Domain Peptides to 14-3-3σ.
ACS Chem Biol. 2020; 15:262-271. doi: 10.1021/acschembio.9b00893.
Medicinal Chemistry ; Biological Chemistry ; Structural Analysis ; Protein-Protein Interactions ; Fragment screens ; Peptides ; Nuclear Magnetic Resonance Spectroscopy