ArticleEuropean journal of medicinal chemistry2019
Hitting on the move: Targeting intrinsically disordered protein states of the MDM2-p53 interaction.
Article in European journal of medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Template-Controlled Mechanochemical Dissociation of a Rotaxane.Angewandte Chemie (International ed. in English) · 2026Article
- Scaffold-hopping for molecular glues targeting the 14-3-3/ERα complex.Nature communications · 2025Article
- Resistance mechanisms to inhibitors of p53-MDM2 interactions in cancer therapy: can we overcome them?Cellular & molecular biology letters · 2021Review
- Development of MDM2 degraders based on ligands derived from Ugi reactions: Lessons and discoveries.European journal of medicinal chemistry · 2021Article
- Therapeutic opportunities in cancer therapy: targeting the p53-MDM2/MDMX interactions.American journal of cancer research · 2021Review
- Roles of DANCR/microRNA-518a-3p/MDMA ceRNA network in the growth and malignant behaviors of colon cancer cells.BMC cancer · 2020Article
- Optimized Inhibitors of MDM2 via an Attempted Protein-Templated Reductive Amination.ChemMedChem · 2020Article
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Intrinsically disordered proteins are an emerging class of proteins without a folded structure and currently disorder-based drug targeting remains a challenge. p53 is the principal regulator of cell division and growth whereas MDM2 consists its main negative regulator. The MDM2-p53 recognition is a dynamic and multistage process that amongst other, employs the dissociation of a transient α-helical N-terminal ''lid'' segment of MDM2 from the proximity of the p53-complementary interface. Several small molecule inhibitors have been reported to inhibit the formation of the p53-MDM2 complex with the vast majority mimicking the p53 residues Phe19, Trp23 and Leu26. Recently, we have described the transit from the 3-point to 4-point pharmacophore model stabilizing this intrinsically disordered N-terminus by increasing the binding affinity by a factor of 3. Therefore, we performed a thorough SAR analysis, including chiral separation of key compound which was evaluated by FP and 2D NMR. Finally, p53-specific anti-cancer activity towards p53-wild-type cancer cells was observed for several representative compounds.
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