| Literature DB >> 17256834 |
Milan Bruncko1, Thorsten K Oost, Barbara A Belli, Hong Ding, Mary K Joseph, Aaron Kunzer, Darlene Martineau, William J McClellan, Michael Mitten, Shi-Chung Ng, Paul M Nimmer, Tilman Oltersdorf, Cheol-Min Park, Andrew M Petros, Alexander R Shoemaker, Xiaohong Song, Xilu Wang, Michael D Wendt, Haichao Zhang, Stephen W Fesik, Saul H Rosenberg, Steven W Elmore.
Abstract
Overexpression of the antiapototic proteins Bcl-2 and Bcl-xL provides a common mechanism through which cancer cells gain a survival advantage and become resistant to conventional chemotherapy. Inhibition of these prosurvival proteins is an attractive strategy for cancer therapy. We recently described the discovery of a selective Bcl-xL antagonist that potentiates the antitumor activity of chemotherapy and radiation. Here we describe the use of structure-guided design to exploit a deep hydrophobic binding pocket on the surface of these proteins to develop the first dual, subnanomolar inhibitors of Bcl-xL and Bcl-2. This study culminated in the identification of 2, which exhibited EC50 values of 8 nM and 30 nM in Bcl-2 and Bcl-xL dependent cells, respectively. Compound 2 demonstrated single agent efficacy against human follicular lymphoma cell lines that overexpress Bcl-2, and efficacy in a murine xenograft model of lymphoma when given both as a single agent and in combination with etoposide.Entities:
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Year: 2007 PMID: 17256834 DOI: 10.1021/jm061152t
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446