Chemistry is par excellence the science of transforming matter, and as such lies at the crossroads between the physical sciences and mathematics on the one hand, and the life sciences, earth sciences and materials sciences on the other. State-of-the-art laboratories, led by world-renowned researchers, are dedicated to a wide range of fields, from organic chemistry to materials chemistry, analytical chemistry and theoretical chemistry.
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Spotlight
Agenda
Public Defense of a Doctoral Dissertation in Chemical Sciences - Gilles Henon
MtSerB2: A Structural Testbed for PPI-Directed Discovery—Structure-Based Virtual Screening Against the ACT Domain Interface of an Essential Mycobacterium tuberculosis Phosphoserine Phosphatase
Jury
- Prof. Steve LANNERS (UNamur), Chair
- Prof. Johan WOUTERS (UNamur), Secretary
- Prof. Pierre FRANCOTTE (ULiège)
- Dr. Marie HAUFROID (UCB)
- Prof. Lionel POCHET (UNamur)
Abstract
Currently, Mycobacterium tuberculosis remains the second deadliest infectious agent in the world, responsible for 1.6 million deaths in 2021. The burden and cost of current treatment (6 months and 4,000 euros), coupled with the alarming emergence of antibiotic-resistant strains, underscore the absolute urgency of developing new therapeutic molecules. This study focuses on the Mycobacterium tuberculosis phosphoserine phosphatase (MtSerB2), an enzyme essential for serine biosynthesis and vital to the pathogen’s survival. Furthermore, this protein plays a key role in host invasion (through its interactions with the NF-κB factor and the cellular cytoskeleton), making MtSerB2 a prime therapeutic target for the development of new, potent anti-tuberculosis drugs.
One of the innovative strategies explored in this thesis is based on destabilizing the protein’s structure (disruption of protein structure). The goal is to design a molecule capable of disrupting the enzyme’s conformation, thereby causing it to lose its catalytic activity. This new class of molecules is expected to exhibit significantly higher selectivity for MtSerB2 compared to its human homolog, human phosphoserine phosphatase (hPSP).
To this end, the Mycobacterium avium phosphoserine phosphatase (MaSerB) was initially used as a model system, justified by its 83% sequence identity with MtSerB2 and its propensity to crystallize rapidly. Initially, a virtual screening of drugs already available on the market was conducted to identify potential inhibitors of MaSerB. Enzymatic assays based on malachite green detection
were then performed to evaluate the inhibitory activity of the various candidates. The results demonstrated increased selectivity of these compounds for dimeric proteins (MtSerB2 and MaSerB) compared to the human enzyme hPSP.
Notably, subsequent enzymatic assays conducted directly on MtSerB2 revealed response profiles that differed from those observed with the MaSerB model. To elucidate the molecular basis of these differences, the structure of the protein in its ligand-bound state is currently being investigated. To this end, protein-inhibitor complexes have been crystallized and will be analyzed by X-ray diffraction.
Public Defense of a Doctoral Dissertation in Chemical Sciences - Martina Saitta
Investigating the relationship between the acidity of heterogeneous catalysts and their activity in ethyl levulinate and glycerol conversions.
Abstract
The development of efficient heterogeneous acid catalysts is essential for the sustainable valorization of biomass-derived platform molecules. This Ph.D. thesis focuses on the design, synthesis, characterization, and catalytic evaluation of novel acidic materials for two representative biomass upgrading reactions: the ketalization of glycerol to solketal and the conversion of ethyl levulinate to γ-valerolactone. Several classes of catalysts were investigated, including Group IV metal-doped mesoporous silica nanotubes and hollow nanospheres, sulfonic acid-functionalized silica materials, and porous metal phosphonates. The aim was to establish relationships between the properties of the catalysts—in particular their acidity—and their catalytic performance.
The results demonstrated that the nature of the metal cation in metal-doped nanostructured silica strongly influences catalyst acidity and reactivity. Furthermore, synthesis parameters such as the loading of the metal cation and the preparation method were shown to control the Lewis/Brønsted ratio and the strength of Lewis acid sites, allowing the tuning of catalytic performance. Materials rich in Lewis acidity preferentially promoted the conversion of ethyl levulinate, while catalysts with higher Brønsted acidity were more effective in glycerol ketalization.
The introduction of sulfonic acid groups significantly enhanced Brønsted acidity and led to extremely active catalysts for solketal production. At the same time, studies on layered phosphonates highlighted the crucial role of the phosphoric spacer in ensuring material stability and enabling their reuse over multiple catalytic cycles. For amorphous porous metal phosphonates, key synthetic parameters—including acid concentration, solvent choice, and the use of a templating agent—were found to significantly influence the acidity of the materials and, consequently, their catalytic activity.
Overall, this work provides valuable insights into structure-acidity-reactivity relationships and offers guidelines for the rational design of heterogeneous acid catalysts for biomass valorization.
Jury
- Prof. Jérémy DEHON (UNamur), Chair
- Prof. Carmela APRILE (UNamur), Secretary
- Prof. Sophie HERMANS (UCLouvain)
- Prof. Damien DEBECKER (UCLouvain)
- Prof. Vera MEYNEN (UAntwerpen)
- Prof. Tatjana PARAC-VOGT (KULeuven)
2nd Symposium on Protein Disorder, Interactions, and Dynamics (PDID)
Following a successful first edition that notably brought together leading figures known for discovering and conceptualizing intrinsically disordered proteins—Drs. Vladimir N. Uversky, Peter Tompa, and Sonia Longhi—we are pleased to announce that the second edition of the One-Day Symposium on Protein Disorder, Interactions, and Dynamics (PDID 2026) will be held on Friday, December 18, 2026, at the University of Namur (UNamur) in Namur, Belgium.
The PDID symposium is finally back in 2026!
Organized every two years by the Belgian Biophysical Society (BBS) and the Laboratoire de Chimie Physique des Biomolécules (CPB), the PDID symposium is an intimate and friendly event for exchanging new ideas and meeting leading experts in the field in the quintessentially Belgian city of Namur, the capital of Wallonia, located at the confluence of the Meuse and Sambre rivers.
We welcome participants from any scientific background who are particularly interested in delving into the world of biomolecular dynamics and exploring their unique behaviors, including structural transitions, interaction networks, protein-ligand interactions, self-assembly, amyloid fibrillation, condensation, phase separation, and phase transitions. Through the lens of biophysics, biochemistry, bioinformatics, and molecular biology, the program aims to cover both experimental and computational approaches for characterizing such intricate and elusive systems in health-related, biotechnological, and biomaterial contexts.