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Current Topics in Medicinal Chemistry

Author(s): Yingge Wang, Yongfang Yao, Hai-Liang Zhu* and Yongtao Duan*

DOI: 10.2174/1568026620999200616132924

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Butterfly Structure: A Privileged Scaffold Targeting Tubulin-Colchicine Binding Site

Page: [1505 - 1508] Pages: 4

  • * (Excluding Mailing and Handling)

Abstract

Butterfly-shaped structure, as a novel scaffold with an attractive and certain shape, has been widely used in new drug discovery. Tubulin, composing of α- and β-tubulin heterodimers, plays a key role in mitosis and cell division which are regarded as an excellent target for cancer therapy. Currently, a series of butterfly shape diaryl heterocyclic compounds have been reported with strong potential against the tubulin-colchicine binding site. It is with one ring buried in the β subunit, another ring interacts with the α subunit and the main body is located in the flat pocket. Here, we firstly introduce the concept of butterfly structure for the tubulin inhibitors, focusing on the latest advancements in a variety of molecules bearing butterfly structure, and then highlight the challenges and future direction of butterfly structure- based tubulin-colchicine binding site inhibitors.

Keywords: Butterfly structure, Cancer, Diaryl heterocyclic, Tubulin-colchicine Binding site, Inhibitors, β-lactam.

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