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Prof. dr. ir. Brunsveld

Luc (Lucas) Brunsveld (1975) received his PhD degree in 2001 under supervision of prof. Bert Meijer at the Eindhoven University of Technology. Topic of the thesis was the self-assembly of designed molecules into helical architectures in water. Subsequently, he moved as a Humboldt fellow to the Max Planck Institute of Molecular Physiologie, Dortmund, to work on the protein semi-synthesis and evaluation of lipidated Ras GTPases in the group of prof. Herbert Waldmann. From 2003-2004 he worked as a group leader in the medicinal chemistry department of Organon (now Schering-Plough) in Oss, on nuclear receptor medicinal chemistry.

End of 2004 Luc Brunsveld received the Sofja Kovalevskaja Award from the Alexander von Humboldt Foundation, with which he established his own research group at the MPI of Molecular Physiologie, Dortmund, beginning 2005, working on the combination of supramolecular chemistry with protein biochemistry and cellular biology, generating new approaches to modulate biological processes. In 2006 he in addition became group leader at the Chemical Genomics Centre of the Max Planck Society, Dortmund, working on the chemical biology of nuclear receptors to understand and modulate the nuclear receptor-cofactor interaction, in close collaboration with Bayer-Schering Pharma, Merck-Serono, and Schering-Plough.

In the middle of 2008 Luc Brunsveld received an ERC starting grant and became full professor in chemical biology in the Department of Biomedical Engineering at the Eindhoven University of Technology.

In his research Luc Brunsveld uses chemical biology approaches to study protein-protein interactions. Two general themes are followed: 1) Supramolecular Architectures are being pursued as instruments to modulate protein-protein interactions and 2) the Nuclear Receptor – Cofactor interaction is being investigated as a specific protein-protein interaction with many unsolved questions, possibly amendable via chemical biology.

  1. Supramolecular architectures are used as tools to control protein-protein interactions. Supramolecular elements are for example selectively attached to proteins to control their dimerization and localization. Self-assembling multivalent architectures are used as scaffolds for the recognition and binding of cells. The combination of supramolecular chemistry with chemical biology is envisioned to enable the modulation of protein-protein interactions in a new fashion and thus provide new entries to this long standing fundamental challenge.
  2. The nuclear receptor – cofactor interaction is a highly relevant protein-protein interaction, regulating the transcription of a large number of genes. One of the goals is to develop compounds that modulate this interaction. These molecular tools are subsequently used to perturb the molecular function of the proteins in the cell. Also, there is a focus on post-translational modifications regulating this interaction, via generation of specifically modified proteins and their application in for example biophysical studies to evaluate these modifications.

More information

Publicaties

Key Publications

Mueller, M.K.; Brunsveld, L.
A Supramolecular Polymer as a Self-Assembling Polyvalent Scaffold
Angew. Chem. Int. Ed. 48, p. 2921-2924 (2009)

Vaz, E.; Pommerantz, W.C.; Geyer, M.; Gellman, S.H.; Brunsveld, L.
Comparison of Design Strategies for Promotion of beta-peptide 14-helix Stability in Water
ChemBioChem 9, p. 2254-2259 (2008)

Wu, Y.; Alexandrov, K.; Brunsveld, L
A high-throughput fluorometric assay for Rab geranylgeranyltransferase
Nature Protocols 2, p. 2704 - 2711 (2007).

Zhang, L.; Wu, Y.; Brunsveld, L.
A synthetic Supramolecular Construct Modulating Protein Assembly in Cells
Angew. Chem. Int. Ed. 46 p. 1798-1802 (2007)

Brunsveld, L.; Kuhlmann, J.; Alexandrov, K.; Wittinghofer, A.; Goods, R.S.;
Waldmann, H.
Lipidated Ras and Rab peptides and proteins – synthesis, structure, and function
Angew. Chem. Int. Ed. 45 p. 6622-6646 (2006)

List of publications and patents 1997 -2008

Contactgegevens

Eindhoven University of Technology
Biomedical Engineering
Chemical Biology
PO Box 513, Helix STO 3.37
5600 MB
Eindhoven, The Netherlands
Tel: +31 40 247 2870