Strategies involved in the construction of two series of novel potent inhibitors of ABL-T315I

MEDI 359

Binqi Zeng1, Jianguo Cao, jcao@targegen.com1, Chun P. Chow, chow@targegen.com1, Chi-Ching Mak, cmak@targegen.com1, Elena Dneprovskaia1, Richard Fine2, Hong Gu3, Ehab Hanna, hanna@targegen.com1, John Hood, jhood@targegen.com1, Xinshan Kang, jasonkang2005@yahoo.com2, Boris Klebansky, bk@biopredict.com2, Ge Li3, Dan Lohse, dlohse@targegen.com1, Andrew McPherson1, Glenn Noronha, gnoronha@targegen.com1, Joel Renick, jrenick@targegen.com1, Moorthy S. S. Palanki, palanki@targegen.com1, Ved P. Pathak, pathak@targegen.com1, Richard Soll, rsoll@targegen.com1, Suhan Tang3, and Hong Zhu, hzhu@targegen.com1. (1) TargeGen, Inc, 9380 Judicial Drive, San Diego, CA 92121, (2) BioPredict, Inc, 660 Kinderkamack Road, Suite 201, Oradell, NJ 07649-1525, (3) Wuxi PharmaTech Co. Ltd, Shanghai, China
Although Gleevec has been a remarkable success for treatment of CML, a significant number of patients develop drug resistance. It is estimated that 50-90% of resistance is drug related and due to mutations that alter the affinity of Gleevec to the mutated enzyme. The T315I (gatekeeper) mutation stands out among the >40 clinically identified mutations because it shows highest prevalence (>20%), and maintains resistance to all recently developed BCR-ABL inhibitors (Tasigna, Sprycel) that target most other mutations. Using molecular modeling, we have developed two series of novel ABL-T315I inhibitors to target the ABL-T315I mutant both in enzyme and cell-based assays. We will present the synthetic strategies that enabled optimizations of nM inhibitors of ABL-T315I in both series.
 

Poster Session
7:00 PM-9:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Medicinal Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007