475272-40-3Relevant academic research and scientific papers
Terphenyl-based Bak BH3 α-helical proteomimetics as low-molecular-weight antagonists of Bcl-xL
Yin, Hang,Lee, Gui-In,Sedey, Kristine A.,Kutzki, Olaf,Park, Hyung Soon,Orner, Brendan P.,Ernst, Justin T.,Wang, Hong-Gang,Sebti, Said M.,Hamilton, Andrew D.
, p. 10191 - 10196 (2007/10/03)
We describe a general method for the mimicry of one face of an α-helix based on a terphenyl scaffold that spatially projects functionality in a manner similar to that of two turns of an α-helix. The synthetic scaffold reduces the flexibility and molecular
Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction
Yin, Hang,Lee, Gui-In,Hyung, Soon Park,Payne, Gregory A.,Rodriguez, Johanna M.,Sebti, Said M.,Hamilton, Andrew D.
, p. 2704 - 2707 (2007/10/03)
(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.
Development of a potent Bcl-xL antagonist based on α-helix mimicry
Kutzki, Olaf,Park, Hyung Soon,Ernst, Justin T.,Orner, Brendan P.,Yin, Hang,Hamilton, Andrew D.
, p. 11838 - 11839 (2007/10/03)
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
