Protein modification: from chemical biology to drug discovery
- Date: Wednesday 22 January 2025, 15:00 – 16:00
- Location: Chemistry LT A (2.15)
- Cost: None
Speaker: Professor Edward (Ed) Tate, GSK Chair in Chemical Biology, Imperial College & Francis Crick Institute
We are delighted to invite you to the SoC seminar of Wednesday, 22 January, 3pm at Chemistry Lecture Theatre A. The speaker is Ed Tate from Imperial College.
Title: "Protein modification: from chemical biology to drug discovery"
Professor Edward (Ed) W. Tate, PhD FSRC FRSB
GSK Chair in Chemical Biology, Imperial College & Francis Crick Institute
Department of Chemistry, Molecular Sciences Research Hub, London, https://www.imperial.ac.uk/tate-group/
Keywords: chemical biology, chemical proteomics, post-translational modification, protein degradation, target identification, drug discovery, activity-based probes
Bio: Ed holds the GSK Chair in Chemical Biology at Imperial College London, and he is a Group Leader at the Francis Crick Institute. Following his PhD (2000) with Steve Ley in Cambridge and postdoctoral research in Paris as an 1851 Fellow and Howard Trust Fellow, he was awarded a BBSRC David Phillips Fellowship in 2006 to start his group at Imperial College. He sits on the advisory boards of several international research institutes and biotechs, and develops new drug discovery technologies with companies including Pfizer, GSK and AstraZeneca. His research has been recognised by awards and Fellowships, most recently the 2019 Sir David Cooksey Translation Prize, the 2020 Corday-Morgan Prize of the RSC, a 2022 Cancer Research UK Programme Award and the 2024 RSC Horizon Prize. In 2023 he was appointed to the GSK Endowed Chair in Chemical Biology at Imperial College. Ed is also the academic founder of several biotechs developing his lab’s research toward clinical applications, including Myricx Bio, which in 2024 raised one of the largest Series A rounds to date for a European biotech.
Research: The Tate lab develops novel chemical biology approaches to enable drug discovery against post-translational modification (PTM) pathways and intractable drug targets, including chemical proteomic target identification, screening technologies, and chemical probe discovery for protein-protein interactions and enzymes modulating PTMs. Recent highlights include the first cell-active activity-based probes (ABPs) for deubiquitinases (DUBs), new tools for analysis and discovery of pathogenic secreted protease activities, and the first comprehensive maps of specific classes of protein lipidation PTM through chemical genetics and proteomics. We are also interested in new modalities, including antibody-PROTAC conjugates and targeted protein degradation.