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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Future Science
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nottingham-464542017-11-07T02:14:15Z http://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 application/pdf en http://eprints.nottingham.ac.uk/46454/1/FMC-2017-0100-accepted.pdf Li, Wenlong and Sun, Honghao and Xu, Shengtao and 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 https://www.future-science.com/doi/10.4155/fmc-2017-0100 doi:10.4155/fmc-2017-0100 doi:10.4155/fmc-2017-0100 |
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Digital Repository |
institution_category |
Local University |
institution |
University of Nottingham Malaysia Campus |
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Nottingham Research Data Repository |
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Online Access |
language |
English |
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. |
format |
Article |
author |
Li, Wenlong Sun, Honghao Xu, Shengtao Zhu, Zheying Xu, Jinyi |
spellingShingle |
Li, Wenlong Sun, Honghao Xu, Shengtao Zhu, Zheying Xu, Jinyi Tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures |
author_facet |
Li, Wenlong Sun, Honghao Xu, Shengtao Zhu, Zheying Xu, Jinyi |
author_sort |
Li, Wenlong |
title |
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_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_sort |
tubulin inhibitors targeting the colchicine binding site: a perspective of privileged structures |
publisher |
Future Science |
publishDate |
2017 |
url |
http://eprints.nottingham.ac.uk/46454/ http://eprints.nottingham.ac.uk/46454/ http://eprints.nottingham.ac.uk/46454/ http://eprints.nottingham.ac.uk/46454/1/FMC-2017-0100-accepted.pdf |
first_indexed |
2018-09-06T13:46:48Z |
last_indexed |
2018-09-06T13:46:48Z |
_version_ |
1610866081454358528 |