Research in Drug Development (RD3)

Pharmacognosy Bioanalysis and Drug Discovery

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Research activities

His research field is the analysis of posttranslational modifications (PTMs) of proteins by mass spectrometry. The targeted PTMs are the oxidative ones (oxidation of tryptophan, tyrosine, lysine, cysteine, …) in the context of chronic inflammation pathologies/oxidative stress like in atherosclerosis/cardiovascular disease. Another type of PTMs that he studies, is the glycosylation. Glycosylation is the most abundant modification of proteins, and in the context of therapeutic proteins, more than 60 % of the currently approved biotherapeutics are glycosylated. His research is also devoted to the development of analytical tools for the other “omics” fields mainly metabolomics and proteomics. He currently develops his research projects in the RD3-PBM unit and the Analytical Platform of the Faculty of Pharmacy

Top ten recent articles

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, mai). 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

The other myeloperoxidase: Emerging functions
Vanhamme, L., Zouaoui Boudjeltia, K., Van Antwerpen, P., & Delporte, C. (2018, juillet). The other myeloperoxidase: Emerging functions Archives of biochemistry and biophysics, 649, 1-14. doi:10.1016/j.abb.2018.03.037

Metabolomics fingerprint of coffee species determined by untargeted-profiling study using LC-HRMS
Souard, F., Delporte, C., Stoffelen, P., Thévenot, E. E., Noret, N., Dauvergne, B., Kauffmann, J.-M., Van Antwerpen, P., & Stevigny, C. (2018, avril). Metabolomics fingerprint of coffee species determined by untargeted-profiling study using LC-HRMS Food chemistry, 245, 603-612. doi:10.1016/j.foodchem.2017.10.022

LC-MS analysis combined with principal component analysis and soft independent modelling by class analogy for a better detection of changes in N-glycosylation profiles of therapeutic glycoproteins.
Planinc, A., Dejaegher, B., Vander Heyden, Y., Viaene, J., Van Praet, S., Rappez, F., Van Antwerpen, P., & Delporte, C. (2017, janvier). LC-MS analysis combined with principal component analysis and soft independent modelling by class analogy for a better detection of changes in N-glycosylation profiles of therapeutic glycoproteins. Analytical and Bioanalytical Chemistry. doi:10.1007/s00216-016-9683-9

Batch-to-batch N-glycosylation Study of Infliximab, Trastuzumab, and Bevacizumab, and Stability Study of Bevacizumab
Planinc, A., Dejaegher, B., Vander Heyden, Y., Viaene, J., Van Praet, S., Rappez, F., Van Antwerpen, P., & Delporte, C. (2017, septembre 01). Batch-to-batch N-glycosylation Study of Infliximab, Trastuzumab, and Bevacizumab, and Stability Study of Bevacizumab European journal of hospital pharmacy, 24(5), 286-292. doi:10.1136/ejhpharm-2016-001022

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, janvier 12). Allosteric regulation of G protein-coupled receptor activity by phospholipids. Nature Chemical Biology, 12(1), 1960, 35-39. doi:10.1038/nchembio.1960

Glycan characterization of biopharmaceuticals: Updates and perspectives.
Planinc, A., Bones, J., Dejaegher, B., Van Antwerpen, P., & Delporte, C. (2016, mai). Glycan characterization of biopharmaceuticals: Updates and perspectives. Analytica chimica acta, 921, 13-27. doi:10.1016/j.aca.2016.03.049

Comparative analysis of monoclonal antibody N-glycosylation using stable isotope labelling and UPLC-fluorescence-MS
Millán Martín, S., Delporte, C., Farrell, A., McLoughlin, N., Bones, J., & Navas Iglesias, N. (2015, mars). Comparative analysis of monoclonal antibody N-glycosylation using stable isotope labelling and UPLC-fluorescence-MS Analyst, 140(5), 1442-1447. doi:10.1039/c4an02345e

Multidomain Human Peroxidasin 1 is a Highly Glycosylated and Stable Homotrimeric High-Spin Ferric Peroxidase.
Soudi, M., Paumann-Page, M., Delporte, C., Pirker, K. K., Bellei, M., Edenhofer, E., Stadlmayr, G., Battistuzzi, G., Zouaoui Boudjeltia, K., Furtmüller, P. G., Van Antwerpen, P., & Obinger, C. (2015, février). Multidomain Human Peroxidasin 1 is a Highly Glycosylated and Stable Homotrimeric High-Spin Ferric Peroxidase. The Journal of biological chemistry. doi:10.1074/jbc.M114.632273

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, février). 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