Postdoc
Joined the Hollfelder group: October 2024
Background and Current Projects: I was trained as a biochemist during my undergraduate and master’s studies. Subsequently, I specialised in protein science and molecular biology during my PhD at Leiden University (Netherlands). My research focuses on understanding proteins' structural basis and functional mechanisms during evolution. My thesis explored the evolutionary adaptability of enzymes and the impact of selection pressures on protein evolution pathways, using β-lactamase as the object. Investigating the evolutionary adaptability of β-lactamase through direct evolution in combination with structural characterization such as crystallography and NMR provides information about the mechanisms of rapid adaptations observed for β lactamases in the clinic. The research makes clear how enzyme kinetics and dynamics vary with different selection pressures and maps the evolutionary path that enzymes may take. The underlying structural mechanisms are established to provide a rationale for the observed effects.
My current research is focused on protease engineering to develop modular platforms that pair proteases with antibodies to direct them to target specific proteins such as the oncogenic protein KARS. By utilizing ultrahigh-throughput screening assays and direct evolution, we will screen extensive protease libraries against therapeutically significant targets, rapidly identifying candidates with the desired specificity and activity and aim to enhance the specificity and therapeutic potential of protease-based treatments, addressing the limitations of existing therapies.
Interests: I have a love for travelling, enjoying jazz music, playing the piano and drawing. I also like doing sports such as Yoga, Zumba, and snowboarding.
Publications
[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. Link.
[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. Link.
[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. Link.
