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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

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Authors

Wenlong Li

Honghao Sun

Shengtao Xu

ZHEYING ZHU Zheying.Zhu@nottingham.ac.uk
Associate Professor in International Pharmacy and Traditional Medicines

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.

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), https://doi.org/10.4155/fmc-2017-0100

Journal Article Type Article
Acceptance Date Aug 20, 2017
Online Publication Date Sep 20, 2017
Deposit Date Sep 18, 2017
Publicly Available Date Sep 21, 2018
Journal Future Medicinal Chemistry
Print ISSN 1756-8919
Electronic ISSN 1756-8927
Publisher Future Science
Peer Reviewed Peer Reviewed
Volume 9
Issue 15
DOI https://doi.org/10.4155/fmc-2017-0100
Keywords Microtubule, Privileged structures, Tubulin inhibitors, Colchicine binding site inhibitors, Colchicine domain, Prodrug
Public URL https://nottingham-repository.worktribe.com/output/883854
Publisher URL https://www.future-science.com/doi/10.4155/fmc-2017-0100
Contract Date Sep 18, 2017

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