UMR8576 – CNRS – University of Lille – Pasteur Institute of Lille
The NMR laboratory is a technical platform of the Pasteur Institute of Lille. The laboratory is equipped with a 600MHz spectrometer with a cryo-probe as well as a 300MHz spectrometer, both equipped with a sample changer.
The 300 MHz low-field spectrometer is dedicated to the analytical control of small molecules, enabling detailed analytical characterization of synthesized compounds or isolated natural products. Users can access it after completing training.
The data obtained from the 600MHz spectrometer support various research projects by enabling:
- Screening of ligand-target protein interactions for medicinal chemistry
- 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 analyses of compounds.
The technical platform is open to hosting academic and industrial users.
News
The CPER longevity program has enabled the installation of next-generation sample changers and consoles for the 300 MHz and 600 MHz spectrometers, allowing for optimal use of all functionalities, particularly the observation of the fluorine nucleus with high sensitivity—an essential element in current and future screening processes for molecules of therapeutic interest. This capability is available to only a very limited number of academic sites in France.
Cross-functional projects
Members
Isabelle LANDRIEU
Unit Director UMR9031
François-Xavier CANTRELLE
IR, University of Lille, Technical Manager
Xavier HANOUILLE
DR, CNRS
Davy SINAEVE
Research Fellow, CNRS
Keywords
Team contact
Isabelle LANDRIEU
Unit Director UMR9031
Publications
Eur J Med Chem. 2020; 200:112440. doi: 10.1016/j.ejmech.2020.112440.
Discovery of the first Mycobacterium tuberculosis MabA (FabG1) inhibitors through a fragment-based screening.
Medchemcomm. 2019; 10:1796-1802. doi:10.1039/c9md00215d.
Set-up and screening of a fragment library targeting the 14-3-3 protein interface.
ACS Chem Biol. 2020; 15:262-271. doi: 10.1021/acschembio.9b00893.
