Benzoquinone ansamycin 17AAG binds to mitochondrial voltage-dependent anion channel and inhibits cell invasion.

@article{Xie2011BenzoquinoneA1,
  title={Benzoquinone ansamycin 17AAG binds to mitochondrial voltage-dependent anion channel and inhibits cell invasion.},
  author={Qian Xie and Robert Wondergem and Yuehai Shen and Greg S. Cavey and Jiyuan Ke and Ryan C Thompson and Robert F Bradley and Jennifer Daugherty-Holtrop and Yong Xu and Edwin Chen and Hanan Omar and Neal Rosen and David Wenkert and Hongjiao Xu and George F. Vande Woude},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 10},
  pages={4105-10}
}
Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function. We discovered that these drugs associate with mitochondria, specifically to the mitochondrial membrane voltage-dependent anion channel (VDAC) via a hydrophobic interaction that is independent of HSP90. In vitro, 17AAG functions as a Ca(2+) mitochondrial regulator similar to benzoquinone-ubiquinones like Ub0. All of these compounds… CONTINUE READING