Research in Drug Development (RD3)

Pharmacognosy Bioanalysis and Drug Discovery

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Research activities

His first research interests focus on the validation of myeloperoxidase as a therapeutical target. In this context, part of his research is also dedicated to the inhibition of myeloperoxidase by chemical screening and rational drug design approach. Since 2008, his main task has been the development of the analytical platform of the Faculty of Pharmacy (ULB) and especially the mass spectrometry. Beside the myeloperoxidase research topic, method validations suitable for the pharmaceutical and biomedical researches are the main part of his actual activities: oxidized peptide quantifications, glycobiology, proteomics, metabolomics, lipidomics, small molecules analysis...

Top ten articles


Targeted and Untargeted Mass Spectrometry-Based Metabolomics for Chemical Profiling of Three Coffee Species

Montis, A., Souard, F., Delporte, C., Stoffelen, P., Stevigny, C., & Van Antwerpen, P. (2022). Targeted and Untargeted Mass Spectrometry-Based Metabolomics for Chemical Profiling of Three Coffee Species. Molecules (Print Archive Edition), 27(10), 3152. doi:10.3390/molecules27103152  

 

Untargeted metabolomics approach to discriminate mistletoe commercial products

Vanhaverbeke, C., Touboul, D., Elie, N., Prévost, M., Meunier, C. C., Michelland, S. S., Cunin, V. V., Ma, L., Vermijlen, D., Delporte, C., Pochet, S., Le Gouellec, A. A., Sève, M. M., Van Antwerpen, P., & Souard, F. (2021). Untargeted metabolomics approach to discriminate mistletoe commercial products. Scientific report, 11, 10.1038/s41598-021-93255-z, 14205.  

 

Validation of a LC/MSMS method for simultaneous quantification of 9 nucleotides in biological matrices.

Cortese, M., Delporte, C., Dufour, D., Noyon, C., Chaumont, M., De Becker, B., Reye, F., Rousseau, A., Eker, O. F., Neve, J., Piagnerelli, M., Zouaoui Boudjeltia, K., Robaye, B., & Van Antwerpen, P. (2019). Validation of a LC/MSMS method for simultaneous quantification of 9 nucleotides in biological matrices. Talanta, 193, 206-214. doi:10.1016/j.talanta.2018.10.003  

 

Native and myeloperoxidase-oxidized low-density lipoproteins act in synergy to induce release of resolvin-D1 from endothelial cells.

Dufour, D., Khalil, A., Nuyens, V., Rousseau, A., Delporte, C., Noyon, C., Cortese, M., Reye, F., Pireaux, V., Neve, J., Vanhamme, L., Robaye, B., Lelubre, C., Desmet, J.-M., Raes, M., Zouaoui Boudjeltia, K., & Van Antwerpen, P. (2018). Native and myeloperoxidase-oxidized low-density lipoproteins act in synergy to induce release of resolvin-D1 from endothelial cells. Atherosclerosis, 272, 108-117. doi:10.1016/j.atherosclerosis.2018.03.012  

 

Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques?

Delporte, C., Zouaoui Boudjeltia, K., Furtmueller, P. G., Maki, R., Dieu, M., Noyon, C., Soudi, M., Dufour, D., Coremans, C., Nuyens, V., Reye, F., Rousseau, A., Raes, M., Moguilevsky, N., Vanhaeverbeek, M., Ducobu, J., Neve, J., Robaye, B., Vanhamme, L., Reynolds, W., Obinger, C., & Van Antwerpen, P. (2018). Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques? The Journal of biological chemistry. doi:10.1074/jbc.M117.801076  

 

Validation of a sensitive LC/MSMS method for chloronucleoside analysis in biological matrixes and its applications

Noyon, C., Delporte, C., Dufour, D., Cortese, M., Rousseau, A., Poelvoorde, P., Neve, J., Vanhamme, L., Zouaoui Boudjeltia, K., Roumeguere, T., & Van Antwerpen, P. (2016). Validation of a sensitive LC/MSMS method for chloronucleoside analysis in biological matrixes and its applications. Talanta, 154, 322-328. doi:10.1016/j.talanta.2016.03.087  

 

Allosteric regulation of G protein-coupled receptor activity by phospholipids.

Dawaliby, R., Trubbia, C., Delporte, C., Masureel, M., Van Antwerpen, P., Kobilka, B. K., & Govaerts, C. (2016). Allosteric regulation of G protein-coupled receptor activity by phospholipids. Nature Chemical Biology, 12(1), 1960, 35-39. doi:10.1038/nchembio.1960  

 

Impact of interaction between myeloperoxidase and low-density lipoprotein on the specific activity of the enzyme and subsequent post-translational oxidative modifications of apolipoprotein B-100.

Delporte, C., Zouaoui Boudjeltia, K., Noyon, C., Furtmueller, P. G., Nuyens, V., Slomianny, M.-C., Madhoun, P., Desmet, J.-M., Raynal, P., Dufour, D., Koyani, C. N., Reye, F., Rousseau, A., Vanhaeverbeek, M., Ducobu, J., Michalski, J.-C., Neve, J., Vanhamme, L., Obinger, C., Malle, E., & Van Antwerpen, P. (2014). Impact of interaction between myeloperoxidase and low-density lipoprotein on the specific activity of the enzyme and subsequent post-translational oxidative modifications of apolipoprotein B-100. Journal of lipid research. doi:10.1194/jlr.M047449  

 

Simultaneous measurement of protein-bound 3-chlorotyrosine and homocitrulline by LC-MS/MS after hydrolysis assisted by microwave: Application to the study of myeloperoxidase activity during hemodialysis.

Delporte, C., Franck, T., Noyon, C., Dufour, D., Rousseau, A., Madhoun, P., Desmet, J.-M., Serteyn, D., Raes, M., Nortier, J., Vanhaeverbeek, M., Moguilevsky, N., Neve, J., Vanhamme, L., Van Antwerpen, P., & Zouaoui Boudjeltia, K. (2012). Simultaneous measurement of protein-bound 3-chlorotyrosine and homocitrulline by LC-MS/MS after hydrolysis assisted by microwave: Application to the study of myeloperoxidase activity during hemodialysis. Talanta, 99, 603-609. doi:10.1016/j.talanta.2012.06.044  

 

Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.

Van Antwerpen, P., Slomianny, M.-C., Zouaoui Boudjeltia, K., Delporte, C., Faid, V., Calay, D., Rousseau, A., Moguilevsky, N., Raes, M., Vanhamme, L., Furtmüller, P. G., Obinger, C., Vanhaeverbeek, M., Neve, J., & Michalski, J.-C. (2010). Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity. The Journal of biological chemistry, 285(21), 16351-16359. doi:10.1074/jbc.M109.089748