14617-30-2Relevant academic research and scientific papers
Aromatic oligoamide foldamers with a "wet edge" as inhibitors of the α-helix-mediated p53-hDM2 protein-protein interaction
Prabhakaran, Panchami,Barnard, Anna,Murphy, Natasha S.,Kilner, Colin A.,Edwards, Thomas A.,Wilson, Andrew J.
, p. 3504 - 3512 (2013)
This paper describes the design, synthesis and structural analysis of a 3-O-alkylated aromatic oligoamide that incorporates an additional hydrophilic 6-O-alkyl substituent in the central monomer. This oligomer exhibits low μM inhibitory potency against th
COMPOUNDS, COMPOSITIONS AND METHODS FOR STABILIZING TRANSTHYRETIN AND INHIBITING TRANSTHYRETIN MISFOLDING
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, (2021/08/06)
Provided herein are compounds having activity against TTR related conditions, and pharmaceutically accepted salts and solvates thereof. Also provided are methods of using the compounds for inhibiting and preventing TTR aggregation and/or amyloid formation in the peripheral nerves, kidney, cardiac tissue, eye and CNS, and of treating a subject with peripheral TTR amyloidosis.
Perturbation of the c-Myc-Max Protein-Protein Interaction via Synthetic α-Helix Mimetics
Jung, Kwan-Young,Wang, Huabo,Teriete, Peter,Yap, Jeremy L.,Chen, Lijia,Lanning, Maryanna E.,Hu, Angela,Lambert, Lester J.,Holien, Toril,Sundan, Anders,Cosford, Nicholas D. P.,Prochownik, Edward V.,Fletcher, Steven
, p. 3002 - 3024 (2015/04/27)
The rational design of inhibitors of the bHLH-ZIP oncoprotein c-Myc is hampered by a lack of structure in its monomeric state. We describe herein the design of novel, low-molecular-weight, synthetic α-helix mimetics that recognize helical c-Myc in its transcriptionally active coiled-coil structure in association with its obligate bHLH-ZIP partner Max. These compounds perturb the heterodimer's binding to its canonical E-box DNA sequence without causing protein-protein dissociation, heralding a new mechanistic class of "direct" c-Myc inhibitors. In addition to electrophoretic mobility shift assays, this model was corroborated by further biophysical methods, including NMR spectroscopy and surface plasmon resonance. Several compounds demonstrated a 2-fold or greater selectivity for c-Myc-Max heterodimers over Max-Max homodimers with IC50 values as low as 5.6 μM. Finally, these compounds inhibited the proliferation of c-Myc-expressing cell lines in a concentration-dependent manner that correlated with the loss of expression of a c-Myc-dependent reporter plasmid despite the fact that c-Myc-Max heterodimers remained intact. (Chemical Equation Presented).
