Dr Jing Sun is a structural biochemist with a research focus on protein evolution and engineering. She completed her PhD at Leiden University, where she investigated the evolutionary adaptability of enzymes under varying selection pressures, using β-lactamase as a model system. By combining structural techniques such as X-ray crystallography and NMR with directed evolution, her work revealed how enzyme kinetics and dynamics are shaped by environmental constraints, providing mechanistic insights into the rapid adaptations observed in clinical settings. She is currently a Post-doctoral Research Associate in the FH Group within the Department of Biochemistry at the University of Cambridge. Her research is focused on developing a modular protease platform that harnesses antibody-directed targeting for therapeutic applications. Specifically, she is engineering proteases to selectively cleave oncogenic proteins such as KRAS, using ultrahigh-throughput screening and directed evolution. This work aims to enhance the specificity and efficacy of protease-based therapies, offering a promising strategy to overcome limitations in current cancer treatments.

Links to online publications, articles or other work

[1]  Sun J., Boyle A.L., Brünle S., Ubbink M. (2024), A low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the β-lactamase BlaC, International Journal of Biological Macromolecules 278: 134665. doi. org/10.1016/j.ijbiomac.2024.134665.

[2]  Sun, J., Chikunova, A., Boyle, A. L., Voskamp, P., Timmer, M., Ubbink, M. (2023). Enhanced activity against a third-generation cephalosporin by destabilization of the active site of a class A beta-lactamase. International Journal of Biological Macromolecules, 250, 126160. DOI: 10.1016/j.ijbiomac.2023.126160

[3]  Sun, J., Curry, D., Yuan, Q., Zhang, X., & Liang, H. (2016). Highly hybridizable spherical nucleic acids by tandem glutathione treatment and polythymine spacing. ACS Applied Materials & Interfaces, 8(19), 12504-12513. DOI: 10.1021/acsami.6b00717

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