Rens de Vries
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 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.
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.
Allosteric small molecule modulators of nuclear receptorsMolecular and Cellular Endocrinology (2019)
Ligand dependent switch from RXR homo- to RXR-NURR1 heterodimerizationACS Chemical Neuroscience (2017)
Structural interface between LRRK2 and 14-3-3 proteinBiochemical Journal (2017)
Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTRProceedings of the National Academy of Sciences of the United States of America (PNAS) (2016)
No ancillary activities