ArticleArchiv der Pharmazie2026
Breaking the Myb-KIX Alliance: Structure-Guided Discovery of Biaryl Hydroxy-Naphthamides as Disruptors of the c-Myb-CBP/p300 KIX Protein-Protein Interaction.
Article in Archiv der Pharmazie, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
The interaction between the transcription factor c-Myb and the CBP/p300 KIX domain is a critical regulatory node in hematopoietic gene expression and an attractive target in MYB-dependent leukemia. Herein, we aimed to identify new small-molecule disruptors of the c-Myb-CBP/p300 KIX protein-protein interaction using integrated in silico and experimental workflow. A focused library of 1143 biaryl hydroxy-naphthamides (naphthanilides) was subjected virtual screening filters yielding five prioritized candidates (C1-C5). Docking showed that all selected compounds occupied the c-Myb-facing groove of the KIX domain and reproduced key interfacial contacts. Subsequent 1000 ns molecular dynamics simulations revealed distinct stability and disruption profiles, with C1 and C4 showing the most favorable combination of stable groove occupancy, protein-protein interface perturbation, and ligand-binding energetics. Free-energy landscape analysis further supported these compounds as the most conformationally stable interfacial binders. Differential MM/PBSA analysis of the protein-protein interface showed that C1 produced the largest predicted weakening of the c-Myb-KIX interaction (ΔΔG
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