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Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures

Li, Wenlong; Sun, Honghao; Xu, Shengtao; Zhu, Zheying; Xu, Jinyi

Authors

Wenlong Li

Honghao Sun

Shengtao Xu

Zheying Zhu zheying.zhu@nottingham.ac.uk

Jinyi Xu



Abstract

The vital roles of microtubule in mitosis and cell division make it an attractive target for antitumor therapy. Colchicine binding site of tubulin is one of the most important pockets that have been focused on to design tubulin-destabilizing agents. Over the past few years, a large number of colchicine binding site inhibitors (CBSIs) have been developed inspired by natural products or synthetic origins, and many moieties frequently used in these CBSIs are structurally in common. In this review, we will classify the CBSIs into classical CBSIs and nonclassical CBSIs according to their spatial conformations and binding modes with tubulin, and highlight the privileged structures from these CBSIs in the development of tubulin inhibitors targeting the colchicine binding site.

Journal Article Type Article
Journal Future Medicinal Chemistry
Print ISSN 1756-8919
Electronic ISSN 1756-8927
Publisher Future Science
Peer Reviewed Peer Reviewed
Volume 9
Issue 15
APA6 Citation Li, W., Sun, H., Xu, S., Zhu, Z., & Xu, J. (in press). Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures. Future Medicinal Chemistry, 9(15), doi:10.4155/fmc-2017-0100
DOI https://doi.org/10.4155/fmc-2017-0100
Keywords Microtubule, Privileged structures, Tubulin inhibitors, Colchicine binding site inhibitors, Colchicine domain, Prodrug
Publisher URL https://www.future-science.com/doi/10.4155/fmc-2017-0100
Copyright Statement Copyright information regarding this work can be found at the following address: http://eprints.nottingh.../end_user_agreement.pdf

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FMC-2017-0100-accepted.pdf (4.3 Mb)
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Copyright Statement
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf





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