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

@article{Orzez2009DecipheringTA,
  title={Deciphering the antitumoral activity of quinacrine: Binding to and inhibition of Bcl-xL.},
  author={Mar Orz{\'a}ez and Laura Mondrag{\'o}n and Alicia Garc{\'i}a-Jare{\~n}o and Silvia Mosul{\'e}n and Antonio Pineda-Lucena and Enr{\'i}que P{\'e}rez-Pay{\'a}},
  journal={Bioorganic & medicinal chemistry letters},
  year={2009},
  volume={19 6},
  pages={
          1592-5
        }
}
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. 
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