475272-33-4

Upstream product

• 475272-16-3 3-benzyl-4-methoxy-benzene-1-boronic acid 
• 434300-54-6 4-(2-cyanoethyl)-2-isobutylphenyl trifluoromethanesulfonate 
• 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 
• 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 
• 475272-04-9 2-(3-isobutyl-4-methoxyphenyl)-4,4,5,5-tetramethyl-[1,3,2]dioxaborolane 
• 475272-20-9 trifluoro-methanesulfonic acid 3-benzyl-4'-(2-cyanoethyl)-2'-isobutyl-biphenyl-4-yl ester 

Downstream Products

• 475094-55-4 3-(3'-Benzyl-4-(carboxymethoxy)-2,3-diisobutyl-1,1':4',1-terphenyl-4-yl)propanoic acid 
• 475272-34-5 3-(3'-benzyl-2,3''-4''-hydroxy-diisobutyl-1,1':4',1''-terphenyl-4-yl)propanenitrile 
• 475272-35-6 3-(3'-benzyl-4''-(cyanomethoxy)-2,3''-diisobutyl-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.

Proteomimetic compounds and methods

The present invention relates to compounds and pharmaceutical compositions which are proteomimetic and to methods for inhibiting the interaction of an alpha-helical protein with another protein or binding site. Methods for treating diseases or conditions which are modulated through interactions between alpha helical proteins and their binding sites are other aspects of the invention.

Development of a potent Bcl-xL antagonist based on α-helix mimicry

The rational design of low-molecular weight ligands that disrupt protein-protein interactions is still a challenging goal in medicinal chemistry. Our approach to this problem involves the design of molecular scaffolds that mimic the surface functionality