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ID: ALA3098110

Journal: Bioorg Med Chem Lett

Title: Modulating the interaction between CDK2 and cyclin A with a quinoline-based inhibitor.

Authors: Deng Y, Shipps GW, Zhao L, Siddiqui MA, Popovici-Muller J, Curran PJ, Duca JS, Hruza AW, Fischmann TO, Madison VS, Zhang R, McNemar CW, Mayhood TW, Syto R, Annis A, Kirschmeier P, Lees EM, Parry DA, Windsor WT.

Abstract: A new class of quinoline-based kinase inhibitors has been discovered that both disrupt cyclin dependent 2 (CDK2) interaction with its cyclin A subunit and act as ATP competitive inhibitors. The key strategy for discovering this class of protein-protein disrupter compounds was to screen the monomer CDK2 in an affinity-selection/mass spectrometry-based technique and to perform secondary assays that identified compounds that bound only to the inactive CDK2 monomer and not the active CDK2/cyclin A heterodimer. Through a series of chemical modifications the affinity (Kd) of the original hit improved from 1 to 0.005μM.

CiteXplore: 24332088

DOI: 10.1016/j.bmcl.2013.11.041