Aromatic Oligoamide Foldamers with a "Wet Edge" as Inhibitors of the α‐Helix‐Mediated p53–hDM2 Protein–Protein Interaction. Issue 17 (8th May 2013)

• Record Type: Journal Article
• Authors: Prabhakaran, Panchami; Barnard, Anna; Murphy, Natasha S.; Kilner, Colin A.; Edwards, Thomas A.; Wilson, Andrew J.
• Other Names: Tomasini Claudia sponsoringEditor.; Juc Ivan sponsoringEditor.; Aitken David J. sponsoringEditor.; Fülöp Ferenc sponsoringEditor.
• Is Part Of: European journal of organic chemistry. Issue 17(2013)
• Page Start: 3504
• Page End: 3512
• Publication Date: 2013-05-08
• Subjects: Proteins -- Bioorganic chemistry -- Amides -- Foldamers; Chemistry, Organic -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1002/ejoc.201300069
• Languages: English
• ISSNs: 1434-193X

Abstract

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 μM inhibitory potency against the p53– h DM2 interaction compared with its unfunctionalised counterpart and significantly improved solubility. Abstract : A 3‐ O ‐alkylated aromatic oligoamide foldamer incorporating an additional and hydrophilic 6‐ O ‐alkyl substituent in the central monomer is shown to have improved solubility, adopt an active binding conformation and disrupt the p53– h DM2 interaction.