475272-22-1

Upstream product

• 434300-54-6 4-(2-cyanoethyl)-2-isobutylphenyl trifluoromethanesulfonate 
• 863508-40-1 (E)-3-(3-Isobutyl-4-methoxy-phenyl)-acrylonitrile 
• 475272-06-1 3-(4-hydroxy-3-isobutylphenyl)propanenitrile 
• 475272-05-0 3-(3-isobutyl-4-methoxyphenyl)propanenitrile 
• 475272-03-8 4-iodo-2-isobutylanisole 
• 475272-20-9 trifluoro-methanesulfonic acid 3-benzyl-4'-(2-cyanoethyl)-2'-isobutyl-biphenyl-4-yl ester 
• 475272-19-6 3-(3'-benzyl-4'-hydroxy-2-isobutyl-1,1'-biphenyl-4-yl)propanenitrile 
• 475272-18-5 3-(3'-benzyl-2-isobutyl-4'-methoxy-1,1'-biphenyl-4-yl)propanenitrile 

Downstream Products

• 475272-23-2 3-(3',3-dibenzyl-4-(cyanomethoxy)-2-isobutyl-1,1':4',1-terphenyl-4-yl)propanenitrile 

Relevant academic research and scientific papers

Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction

(Chemical Equation Presented) HDM2 regulates p53 by binding to its transactivation domain and promoting its ubiquitin-dependent degradation. Crystallographic analysis of the HDM2/p53 complex revealed that three hydrophobic residues (F19, W23, L26) along one face of the p53 helical peptide are essential for binding (see picture). Terphenyl-based antagonists mimic the α-helical region of p53 and disrupt HDM2/p53 complexation.