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ID: ALA2424535

Journal: Bioorg Med Chem Lett

Title: Fragment-based discovery of focal adhesion kinase inhibitors.

Authors: Grädler U, Bomke J, Musil D, Dresing V, Lehmann M, Hölzemann G, Greiner H, Esdar C, Krier M, Heinrich T.

Abstract: Chemically diverse fragment hits of focal adhesion kinase (FAK) were discovered by surface plasmon resonance (SPR) screening of our in-house fragment library. Site specific binding of the primary hits was confirmed in a competition setup using a high-affinity ATP-site inhibitor of FAK. Protein crystallography revealed the binding mode of 41 out of 48 selected fragment hits within the ATP-site. Structural comparison of the fragment binding modes with a DFG-out inhibitor of FAK initiated first synthetic follow-up optimization leading to improved binding affinity.

CiteXplore: 23973211

DOI: 10.1016/j.bmcl.2013.07.050