Rens de Vries started as a doctoral candidate at the Eindhoven University of Technology in September 2016 under the supervision of prof. Luc Brunsveld. In his research, he is exploring how small molecules influence the behavior of nuclear receptors, especially their effects on dimerization and cofactor recruitment. Nuclear receptors regulate the expression of specific genes, thereby controlling our development, homeostasis and metabolism. In multiple diseases, such as neurodegenerative diseases and cancer, the nuclear receptor function is altered. Selectively targeting these nuclear receptors and restoring their behavior, is very interesting in drug discovery. In the human body, processes such as dimerization and cofactor recruitment of these receptors are tightly and selectively mediated. How nature accomplished such a high degree of control is still poorly understood. Making use of protein crystallography, assay development and computational approaches, Rens tries to make his contribution to understand this interesting phenomenon and to potentially exploit it.
If we desire the same level of precision as nature in drug development, we should not be interested in whether a drug works, we should strive to understand why it works.
Rens de Vries (1993) received his Bachelor and Master degree in Biomedical Engineering at Eindhoven University of Technology (TU/e) in 2014 and 2016 respectively. During his master, he performed research in the group of prof. dr. ir. Luc Brunsveld, under the direct supervision of dr. Christian Ottmann. In this research, the interaction between two proteins, important in Parkinson’s disease, was analyzed and quantified. This research was continued during his internship at the Lead Discovery Center GmbH in Dortmund where High-Throughput Screening and Assay Development were used to find drug candidates for this interaction. In 2016, he started as a PhD candidate under the supervision of prof. dr. ir. Luc Brunsveld in the field of Chemical Biology. In his research, he analyses how ligand design can fundamentally change the behavior of nuclear receptors.
Indazole MRL-871 interacts with PPARγ via a binding mode that induces partial agonismBioorganic and Medicinal Chemistry (2022)
Structure-Activity Relationship Studies of Trisubstituted Isoxazoles as Selective Allosteric Ligands for the Retinoic-Acid-Receptor-Related Orphan Receptor γtJournal of Medicinal Chemistry (2021)
Cooperativity between the orthosteric and allosteric ligand binding sites of RORγtProceedings of the National Academy of Sciences of the United States of America (2021)
Structural elucidation of novel allosteric regulatory mechanisms in nuclear receptors(2020)
Elucidation of an allosteric Mode of Action for a Thienopyrazole RORγt Inverse AgonistChemMedChem (2020)
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