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Aromatic Oligoamide Foldamers with a “Wet Edge” as Inhibitors of the α‐Helix‐Mediated p53–<i>h</i>DM2 Protein–Protein Interaction
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Citations
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References
2013
Year
EngineeringProtein AssemblyMolecular BiologyOrganic ChemistryChemistryDiversity Oriented SynthesisProtein FoldingStereoselective SynthesisMolecular RecognitionBiochemistryDiversity-oriented SynthesisAromatic Oligoamide FoldamersMolecular ModelingAdditional Hydrophilic 6‐Structural BiologyNatural SciencesStructural AnalysisCentral MonomerMolecular DockingSynthetic Chemistry
Abstract 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 μ M inhibitory potency against the p53– h DM2 interaction compared with its unfunctionalised counterpart and significantly improved solubility.
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