Professor of Chemical Biology and Fellow of Trinity Hall College (University of Cambridge); Group Leader (Instituto de Medicina Molecular, Lisbon)
University of Cambridge
Recognized for: Groundbreaking research in the area of ‘bench-to-clinic’ bioorthogonal chemistry, which involves the control of tailored chemical reactions that can take place in the body without interfering with natural processes. This revolutionary translational research holds great promise for new breakthroughs in gene editing, labeling of specific proteins in living cells, and the development of new therapeutics.
Areas of Research Interest and Expertise: Bioorthogonal Chemistry, Cancer Biology, Targeting, Protein Chemistry, Nucleic Acid Chemistry
MSci, University of Lisbon, Portugal DPhil, University of Oxford, UK Marie Curie Fellow, Max Planck Institute of Colloids and Interfaces, Germany EMBO Fellow, Swiss Federal Institute of Technology (ETH), Switzerland
Research Summary: In chemistry, the term chemoselectivity refers to the preference for a reagent—a reactive chemical species—to react with one specific chemical entity over a group of alternative reaction pathways. Organic chemists have exploited this property to develop new catalysts and streamline the chemical synthesis of complex synthetic targets. Gonçalo Bernardes, DPhil, is a chemical biologist who uses his background in organic chemistry to harness the intrinsic reactivity of specific functional groups within biological macromolecules like DNA, RNA, and proteins to create biological probes and novel therapeutic agents.
Bernardes has developed a number of bioorthogonal tools—chemical species that can react in live cells without interfering with native processes—that allow the manipulation of biological macromolecules using small molecule probes. One example is Click-Seq, a method that can be used to edit and analyze RNA modifications directly in cells. Click-Seq uses “click chemistry” to install a small molecule RNA degrader directly on RNA to allow mapping and degradation of specific RNA modifications. Bernardes has also established a series of reactions that are chemoselective for lysine and cysteine amino acids within proteins, which allows him to selectively modify the most reactive sites within a protein. The site-selective chemical modification of proteins is a valuable tool for a variety of reasons, and has already proven useful in the modulation of protein activity, delivery of targeted therapeutics, and tagging with fluorogenic probes. These groundbreaking studies and others will continue to yield novel information and spark an endless stream of translational, bench-to-clinic, research.
"I am humbled and grateful that the work of my research group has been recognised with this award. We bridge disciplines to develop new chemical tools to provide fundamental biological knowledge and design the next-generation of targeted therapeutics."
Conde, R.A. Pumroy, C. Baker, T. Rodrigues, A. Guerreiro, B.B. Sousa, M.C. Marques, B.P. de Almeida, S. Lee, E.P. Leites, D. Picard, A. Samanta, S.H. Vaz, S. Sieglitz, M. Langini, M. Remke, R. Roque, T. Weiss, M. Weller, Y. Liu, S. Han, F. Corzana, V.A. Morais, C.C. Faria, T. Carvalho, P. Filippakopoulos, B. Snijder, N.L. Barbosa-Morais, V.Y. Moiseenkova-Bell, G.J.L. Bernardes. Allosteric Antagonist Modulation of TRPV2 by Piperlongumine Impairs Glioblastoma Progression. ACS Central Science, 2021.