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Deciphering the antitumoral activity of quinacrine: Binding to and inhibition of Bcl-xL

2009; Elsevier BV; Volume: 19; Issue: 6 Linguagem: Inglês

10.1016/j.bmcl.2009.02.020

1464-3405

Mar Orzáez, Laura Mondragón, Alicia Belén García-Jareño, Silvia Mosulén, Antonio Pineda‐Lucena, Enríque Pérez‐Payá,

Ion channel regulation and function

From the screening of a unique collection of 880 off-patent small organic molecules, we have found that quinacrine inhibits the interaction between a BH3 domain-derived peptide and the antiapoptotic protein Bcl-xL. Nuclear magnetic resonance spectroscopy confirmed that quinacrine binds to the hydrophobic groove that Bcl-xL uses for interacting with the BH3 domain of proapoptotic proteins. This activity can contribute to the anticancer activity of quinacrine.