Congratulations to Zsofia on winning Best Oral Presentation at the School of Chemistry Postdoctoral Conference on 15th Dec 2017.
Her presentation titled ‘Ligand-Directed Dynamic Combinatorial Chemistry for Inhibition of Protein-Protein Interactions’ outlined the development of a dynamic covalent chemistry approach using peptide-small molecule hybrid structures for targeting protein-protein interactions.
Zsofia is a postdoctoral research fellow working with Thomas Edwards and Andy Wilson. She is funded through a personal EU Horizon 2020 Marie Curie Individual Fellowship that started in May 2017, having initially joined the group on the PoPPI programme. Her fellowship Scaffold Hybridization Approach to Protein-Protein Interactions research focuses on the design and structural characterization of protein-protein interaction inhibitors comprising natural and non-natural components. Zsofia joined the group following a PhD thesis at the University of Szeged (Hungary), where she worked on the design, synthesis and structural characterization of bioactive α/β-peptide β-sheet mimetics, under the supervision of Prof Tamas Martinek.
Zsofia’s presentation outlined the development of a state-of-the-art analytical method based on mass-spectrometry to allow characterization of dynamic combinatorial libraries. The approach allows simultaneous characterization/ identification and relative quantitation of significant numbers of library members in a single experiment. Her presentation was recognized for its clarity in explaining a number of diverse concepts and the breadth and scope of experimental work carried out, comprising, protein expression and characterization, fluorescence anisotropy assay development, synthesis of dynamic combinatorial libraries and mass-spectrometry analyses.
Andy Wilson says, “This prize is recognition of Zsofi’s intellectual creativity and outstanding experimental skill during a highly productive first year with our team: she has set the stage to deliver a really exciting advance in identification inhibitors of topologically and topographically distinct protein-protein interactions that the community cannot currently address.’’