
Caroline TOKARSKI (Pr, University of Bordeaux)
The research activities of the M3S team focus on innovative developments in mass spectrometry for proteomics, structural analysis, and imaging, as well as their applications in life sciences and materials science.
We offer a comprehensive analytical strategy to identify and/or quantify molecules of varying size and complexity (intact compounds as well as subunits) in their native or modified state, both chemically and enzymatically.
These various development axes are supported by a state-of-the-art technical platform featuring complementary ionization sources, high-resolution and high-sensitivity analyzers, and an adaptive bioinformatics tool for optimal exploitation of large datasets.
Home » Multi-scale and Multi-omics Mass Spectrometry (M3S)
Developments in Proteomic Analysis
Advances in proteomic analysis integrate innovative methodologies in both bottom-up and top-down proteomics, employ alternative fragmentation modes for sequencing, and implement comparative/quantitative differential strategies to decipher dynamic and complex biological systems.
Minimally Invasive -Omic Analysis and Trace Analysis
Special attention is given to the development of minimally invasive and highly sensitive sampling methods, in order to preserve the integrity of the treated sample and enable analysis at trace levels.
These approaches are applied to the analysis of a wide variety of biomolecules (proteins, peptides, polysaccharides, lipids, synthetic chemical compounds). They also extend to the analysis of cultural heritage samples (artworks and museum objects, archaeological artifacts).
Identification and Understanding of Bacterial Biofilms, Formation, and Control Methods
This research theme focuses on biofilms, bacteria, attachment phases, culturomics, antibiosis, and enzybiotics.
Our cross-disciplinary expertise in these areas includes:
Proteomics
Bacterial Biofilms & Immobilization Systems
Environmental Pathogens and Bacteriobiotics
Isolation and Phenotyping
Anti-biofilm Products
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Structural analysis leverages the performance of the platform’s instruments (sub-ppm measurement precision, very high resolution, high-mass detection) to elucidate the fine structure of molecules and characterize their modifications.
Within this framework, we focus on the conformation and dynamics of these proteins, their protein–protein and protein–ligand interactions, as well as chemical, co-, and post-translational modifications. These structural studies are applicable both to life sciences and to ancient biomolecules.
Our main actionable approaches include:
Analysis of chemical modifications and PTMs
Cross-linking coupled with mass spectrometry (XL-MS)
Hydrogen/deuterium exchange coupled with mass spectrometry (HDX-MS)
Activity-based protein profiling (ABPP)
Mass spectrometry imaging (MSI) is applied to health (tuberculosis, cancer, asthma, bacteria, etc.) and cultural heritage (organic macromolecules, low-molecular-weight compounds, etc.).
Multimodal imaging is based on mass spectrometry imaging combined with complementary modalities (immunohistochemistry, magnetic resonance imaging, vibrational spectroscopies, etc.).
We develop strategies for both MSI data processing and multimodal imaging.
This research axis relies on our expertise in the following areas:
Matrix-Assisted Laser Desorption/Ionization (MALDI)
Mass spectrometry imaging (MSI)
Multi-omics and multimodal imaging
Immunohistochemistry (IHC)
Data processing
Caroline
TOKARSKI
Professor
University of Bordeaux
Kathell
BATHANY
Research Engineer
University of Bordeaux
Stéphane
CHAIGNEPAIN
Research Engineer
CNRS
Nicolas
DESBENOIT
Research Scientist
CNRS
Boutayna
FRIH
Associate Professor University of Bordeaux
Caroline
LE SÉNÉCHAL
Technician
University of Bordeaux
Bertrand
THOMAS
Research Engineer
CNRS
Sébastien
VILAIN
Professor
Bordeaux INP
Bibliographie
Bibliographie
Bibliographie
MSB
5 groupes de recherche
NMFAB
3 groupes de recherche
CBSC
5 groupes de recherche
Nos enseignants-chercheurs participe à la formation des élèves ingénieurs de Bordeaux INP (ENSMAC, ENSTBB…) et de l’université de Bordeaux.