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[Thermodynamics of calmodulin and tubulin binding to the vinca-alkaloid vinorelbine].

Abstract : Vinca-alkaloids, such as vinblastine, and some of their derivatives, as for example vinorelbine, are widely used in clinical therapy of leukemia and several types of tumors. Their effects are associated with the disfunctioning of the mitotic spindle, which leads to mitosis blockage and a shutdown of the cell cycle. Their primary target is tubulin, however recent research has shown that some of the vinca-alkaloids inhibit calmodulin binding to its targets. Vinka-alkaloids binding with other proteins could be responsible for their efficiency and neuroprotection. Here we investigated the thermodynamics of vinorelbine interactions with calmodulin and tubulin. It was determined that unlike the other vinca-alkaloids both vinorelbine binding sites are located in the C-domain of calmodulin, and characterized by association constants of 4.0 x 10(5) and 5.4 x 10(4) M(-1). At the same time the thermodynamics of vinorelbine binding to tubulin are not much different from that of other vinca-alkaloids. These results will allow getting a better insight on the reaction mechanisms of vinca-alkaloids on a secondary protein target.
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Contributor : Ludovic Leloup Connect in order to contact the contributor
Submitted on : Tuesday, April 3, 2018 - 10:23:41 AM
Last modification on : Tuesday, May 17, 2022 - 2:58:09 PM


  • HAL Id : hal-01756863, version 1
  • PUBMED : 21954603



Philipp O Tsvetkov, A Kulikova, François Devred, E Iu Zerniĭ, D. Lafitte, et al.. [Thermodynamics of calmodulin and tubulin binding to the vinca-alkaloid vinorelbine].. Молекулярная биология / Molecular Biology, Springer Verlag (Germany), 2011, pp.697-702. ⟨hal-01756863⟩



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