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The protein Survivin is highly upregulated in most cancers and considered to be a key player in carcinogenesis. We explored a supramolecular approach to address Survivin as a drug target by inhibiting the protein-protein interaction of Survivin and its functionally relevant binding partner Histone H3. Ligand L1 is based on the guanidiniocarbonyl pyrrole cation and serves as a highly specific anion binder in order to target the interaction between Survivin and Histone H3. NMR titration confirmed binding of L1 to Survivin's Histone H3 binding site. The inhibition of the Survivin-Histone H3 interaction and consequently a reduction of cancer cell proliferation were demonstrated by microscopic and cellular assays. © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.


Cecilia Vallet, Dennis Aschmann, Christine Beuck, Matthias Killa, Annika Meiners, Marcel Mertel, Martin Ehlers, Peter Bayer, Carsten Schmuck, Michael Giese, Shirley K Knauer. Functional Disruption of the Cancer-Relevant Interaction between Survivin and Histone H3 with a Guanidiniocarbonyl Pyrrole Ligand. Angewandte Chemie (International ed. in English). 2020 Mar 27;59(14):5567-5571

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PMID: 31916356

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