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

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 colchic...

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Main Authors: Li, Wenlong, Sun, Honghao, Xu, Shengtao, Zhu, Zheying, Xu, Jinyi
Format: Article
Published: Future Science 2017
Subjects:
Online Access:https://eprints.nottingham.ac.uk/46454/
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author Li, Wenlong
Sun, Honghao
Xu, Shengtao
Zhu, Zheying
Xu, Jinyi
author_facet Li, Wenlong
Sun, Honghao
Xu, Shengtao
Zhu, Zheying
Xu, Jinyi
author_sort Li, Wenlong
building Nottingham Research Data Repository
collection Online Access
description 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.
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spelling nottingham-464542020-05-04T19:08:01Z https://eprints.nottingham.ac.uk/46454/ Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures Li, Wenlong Sun, Honghao Xu, Shengtao Zhu, Zheying Xu, Jinyi 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. Future Science 2017-09-20 Article PeerReviewed Li, Wenlong, Sun, Honghao, Xu, Shengtao, Zhu, Zheying and Xu, Jinyi (2017) Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures. Future Medicinal Chemistry, 9 (15). ISSN 1756-8927 Microtubule Privileged structures Tubulin inhibitors Colchicine binding site inhibitors Colchicine domain Prodrug https://www.future-science.com/doi/10.4155/fmc-2017-0100 doi:10.4155/fmc-2017-0100 doi:10.4155/fmc-2017-0100
spellingShingle Microtubule
Privileged structures
Tubulin inhibitors
Colchicine binding site inhibitors
Colchicine domain
Prodrug
Li, Wenlong
Sun, Honghao
Xu, Shengtao
Zhu, Zheying
Xu, Jinyi
Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title_full Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title_fullStr Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title_full_unstemmed Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title_short Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
title_sort tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures
topic Microtubule
Privileged structures
Tubulin inhibitors
Colchicine binding site inhibitors
Colchicine domain
Prodrug
url https://eprints.nottingham.ac.uk/46454/
https://eprints.nottingham.ac.uk/46454/
https://eprints.nottingham.ac.uk/46454/