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

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

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