475272-05-0Relevant articles and documents
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.
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
Proteomimetic compounds and methods
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, (2008/06/13)
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.