Baud, Matthias - University of Southampton

个人简介

Matthias obtained his BSc from the Université de Besançon (France) in 2003 and MSc from the Ecole Polytechnique Fédérale de Lausanne in 2005. He then moved to the UK to undertake PhD studies at Imperial College London under Dr Matthew Fuchter, working on the development of new chemical probes for epigenetics. After obtaining his PhD in 2011, he moved to the University of Cambridge to work with Dr Alessio Ciulli, followed by a short stay at the School of Life Sciences at the University of Dundee. In 2013 he obtained a MRC Career Development Fellowship to be held at the Laboratory of Molecular Biology in Cambridge, within the group of Professor Sir Alan Fersht. He joined the School of Chemistry at the University of Southampton in September 2016.

研究领域

Cellular processes are mediated by numerous complex and intricate biochemical pathways, involving thousands of biomolecules interacting with each other both in a temporal and spatial manner. As such, probing the spatiotemporal roles and interactome of a biomolecule in its native environment remains a formidable challenge. Despite the continuous progress in omics and structural biology techniques, our understanding of how proteins interact with each other and achieve their downstream physiological effects remains in its infancy. In particular, protein-protein interactions (PPIs) have received a great deal of attention lately, and opened new perspectives for therapeutic interventions through their modulation. Studying PPIs is a difficult task, notably due to the size of the macromolecular assembly (e.g. several MDa), the highly dynamic nature of protein-protein association, the structural adaptability of their interfaces to allow such association, and the dependence of such association on post-translational modifications (PTMs), which are themselves dynamic and regulated by many other proteins. Despite such obstacles, small synthetic molecules can be rationally devised to perturb protein’s interactome by potently binding to their surface. They therefore offer a powerful tool towards functional elucidation and for further therapeutic applications. Small molecules can bind and interact with a protein in many ways. Historically, the vast majority of small molecule chemical probes and drugs were developed with the aim of perturbing the association equilibria between a protein and its partners (e.g. a co-factor or another protein). However, novel and powerful chemical approaches aiming at modulating protein functions with small molecules have emerged in recent years, opening new perspectives in biology and drug discovery.

近期论文

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A bump-and-hole approach to engineer controlled selectivity of BET bromodomain chemical probes - Baud, M. G.J., Lin-Shiao, E., Cardote, T., Tallant, C., Pschibul, A., Chan, K.-H., Zengerle, M., Garcia, J.R., Kwan, T.T.- L., Ferguson, F.M. and Ciulli, A. Published:2014Publication:ScienceVolume:346, (6209)Page Range:638-641doi:10.1126/science.1249830 New synthetic routes to triazolo-benzodiazepine analogues: expanding the scope of the bump-and-hole approach for selective bromo and extra-terminal (bet) bromodomain inhibition - Baud, Matthias, Lin-Shiao, Enrique, Zengerle, Michael, Tallant, Cynthia and Ciulli, Alessio Published:2015Publication:Journal of Medicinal ChemistryVolume:59, (4)Page Range:1492-1500doi:10.1021/acs.jmedchem.5b01135 Exploiting transient protein states for the design of small-molecule stabilizers of mutant p53 - Joerger, Andreas C., Bauer, Matthias R., Wilcken, Rainer, Baud, Matthias, Harbrecht, Hannes, Exner, Thomas E., Boeckler, Frank M., Spencer, John and Fersht, Alan R. Published:2015Publication:Structure Volume:23, (12)Page Range:2246-2255doi:10.1016/j.str.2015.10.016PMID:26636255 Harnessing fluorine–sulfur contacts and multipolar interactions for the design of p53 mutant Y220C rescue drugs - Bauer, Matthias R., Jones, Rhiannon N., Baud, Matthias, Wilcken, Rainer, Boeckler, Frank M., Fersht, Alan R., Joerger, Andreas C. and Spencer, John Published:2016Publication:ACS Chemical BiologyVolume:11, (8)Page Range:2265-2274doi:10.1021/acschembio.6b00315