NDLI: Thermodynamics of calmodulin and tubulin binding to the vinca-alkaloid vinorelbine

Content Provider	Springer Nature Link
Author	Tsvetkov, P. O. Kulikova, A. A. Devred, F. Zernii, E. Yu. Lafitte, D. Makarov, A. A.
Copyright Year	2011
Abstract	Vinca-alkaloids, such as vinblastine, and some of their derivatives, 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 shutting down 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. Vinca-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 they are characterized by association constants of 4.0 × 10$^{5}$ and 5.4 × 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 us to get a better insight on the reaction mechanisms of vinca-alkaloids on a secondary protein target.
Starting Page	641
Ending Page	646
Page Count	6
File Format	PDF
ISSN	00268933
Journal	Molecular Biology
Volume Number	45
Issue Number	4
e-ISSN	16083245
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2011-08-05
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	tubulin calmodulin vinorelbine microtubules Biochemistry Life Sciences Human Genetics
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biophysics

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