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- W2897937537 abstract "Abstract New chemical inhibitors of protein–protein interactions are needed to propel advances in molecular pharmacology. Peptoids are peptidomimetic oligomers with the capability to inhibit protein-protein interactions by mimicking protein secondary structure motifs. Here we report the in silico design of a macrocycle primarily composed of peptoid subunits that targets the β-catenin:TCF interaction. The β-catenin:TCF interaction plays a critical role in the Wnt signaling pathway which is over-activated in multiple cancers, including prostate cancer. Using the Rosetta suite of protein design algorithms, we evaluate how different macrocycle structures can bind a pocket on β-catenin that associates with TCF. The in silico designed macrocycles are screened in vitro using luciferase reporters to identify promising compounds. The most active macrocycle inhibits both Wnt and AR-signaling in prostate cancer cell lines, and markedly diminishes their proliferation. In vivo potential is demonstrated through a zebrafish model, in which Wnt signaling is potently inhibited." @default.
- W2897937537 created "2018-10-26" @default.
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- W2897937537 date "2018-10-23" @default.
- W2897937537 modified "2023-10-13" @default.
- W2897937537 title "Design of Peptoid-peptide Macrocycles to Inhibit the β-catenin TCF Interaction in Prostate Cancer" @default.
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- W2897937537 doi "https://doi.org/10.1038/s41467-018-06845-3" @default.
- W2897937537 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6199279" @default.
- W2897937537 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30352998" @default.
- W2897937537 hasPublicationYear "2018" @default.
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