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Direct inhibition of the NOTCH transcription factor complex
Open accessAbstract
Direct inhibition of transcription factor complexes remains a central challenge in the discipline of ligand discovery. In general, these proteins lack surface involutions suitable for high-affinity binding by small molecules. Here we report the design of synthetic, cell-permeable, stabilized alpha-helical peptides that target a critical protein-protein interface in the NOTCH transactivation complex. We demonstrate that direct, high-affinity binding of the hydrocarbon-stapled peptide SAHM1 prevents assembly of the active transcriptional complex. Inappropriate NOTCH activation is directly implicated in the pathogenesis of several disease states, including T-cell acute lymphoblastic leukaemia (T-ALL). The treatment of leukaemic cells with SAHM1 results in genome-wide suppression of NOTCH-activated genes. Direct antagonism of the NOTCH transcriptional program causes potent, NOTCH-specific anti-proliferative effects in cultured cells and in a mouse model of NOTCH1-driven T-ALL.
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Metadata
- Authors
- Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E.
- Affiliations
- Broad Institute (US)
- Brigham and Women's Hospital (US)
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Verdine, Gregory L.
- Bradner, James E.
- ORCID
- Venue
- Nature
- Published
- 2009-11-12
- Volume
- 462
- Issue
- 7270
- Pages
- 182-188
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2951323
- OpenAlex
- W2085948054
- Cited by
- 752
- References
- 51
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 12 · 2023: 30 · 2022: 21 · 2021: 28 · 2020: 43 · 2019: 35 · 2018: 47 · 2017: 43 · 2016: 34 · 2015: 56 · 2014: 70 · 2013: 76 · 2012: 75
- FWCI
- 32.31
- Type
- journal article
- Language
- en
- Update notices
- erratum (2010-01-21)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Iris (University of Trento) (submittedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22, 5t32gm007598-41)
- National Cancer Institute (N01CO12400, N01-CO-012400, P01CA119070, R01CA092433, R56CA092433)
- National Institute of General Medical Sciences (5T32GM007598, T32-GM007598)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- Notch signaling, hydrocarbon-stapled peptides, protein-protein interaction inhibition, T-cell acute lymphoblastic leukemia, Notch1, transcription factor antagonism, cell-permeable peptide
- MeSH terms
- Animals, Binding, Competitive, Cell Membrane Permeability, Disease Models, Animal, DNA-Binding Proteins, Humans, Models, Molecular, Nuclear Proteins, Peptides, Protein Binding, Substrate Specificity, Transcription Factors, Signal Transduction, Transcriptional Activation, Gene Expression Regulation, Neoplastic, Genome, Protein Structure, Secondary, Protein Structure, Tertiary, Drosophila Proteins, Cell Line, Tumor, Cell Proliferation, Mice, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Receptor, Notch1, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
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