475272-69-6Relevant articles and documents
Relaxation of the rigid backbone of an oligoamide-foldamer-based α-helix mimetic: Identification of potent Bcl-xL inhibitors
Yap, Jeremy L.,Cao, Xiaobo,Vanommeslaeghe, Kenno,Jung, Kwan-Young,Peddaboina, Chander,Wilder, Paul T.,Nan, Anjan,MacKerell, Alexander D.,Smythe, W. Roy,Fletcher, Steven
, p. 2928 - 2933 (2012/05/07)
By conducting a structure-activity relationship study of the backbone of a series of oligoamide-foldamer-based α-helix mimetics of the Bak BH3 helix, we have identified especially potent inhibitors of Bcl-xL. The most potent compound has a Ki value of 94 nM in vitro, and single-digit micromolar IC50 values against the proliferation of several Bcl-xL-overexpressing cancer cell lines. The Royal Society of Chemistry 2012.
Design and application of an α-helix-mimetic scaffold based on an oligoamide-foldamer strategy: Antagonism of the Bak BH3/Bcl-xL complex
Ernst, Justin T.,Becerril, Jorge,Park, Hyung Soon,Yin, Hang,Hamilton, Andrew D.
, p. 535 - 539 (2007/10/03)
The prevention of cell death by the antiapoptotic protein Bcl-xL has been linked to a number of cancers. Bcl-xl binds to the BH3 domain of the proapoptotic protein Bak, thus preventing programmed cell death. A competitive assay and docking studies have shown that the polyamide scaffold 1, which was synthesized based on a rational structure-based design, interferes with the Bak BH3/Bcl-xl complexation.