期刊
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
卷 126, 期 -, 页码 384-407出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.ejmech.2016.11.029
关键词
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资金
- Marie Curie FP7Reintegration-Grants within the 7th European Community Framework Programme
- project operated within the Foundation for Polish Science TEAM Programme
- EU European Regional Development Fund
- Polish National Centre of Science [Symphony-2-UM0-2014/12/W/NZ1/00457]
- National Centre of Science [UMO-2014/12/T/ST5/00684]
- European Regional Development Fund in the framework of the Polish Innovation Economy Operational Program [POIG.02.01.00-12-023/08]
- NIH [1R01GM097082]
- Innovative Medicines Initiative [115489]
- Faculty of Biochemistry, Biophysics and Biotechnology of Jagiellonian University
- Leading National Research Centre (KNOW)
- Ministry of Science and Higher Education
Using the computational pharmacophore-based ANCHOR.QUERY platform a new scaffold was discovered. Potent compounds evolved inhibiting the protein-protein interaction p53-MDM2. An extensive SAR study was performed based on our four-point pharmacophore model, yielding derivatives with affinity to MDM2 in the nanomolar range. Their binding affinity with MDM2 was evaluated using both fluorescence polarization (FP) assay and 2D-NMR-HSQC experiments. 2016 Published by Elsevier Masson SAS.
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