Document Type

Article

Publication Date

6-10-2014

Publication Title

European Journal of Medicinal Chemistry

Abstract

Tubulin and heat shock protein 27 (Hsp27) are well-characterized molecular targets for anti-cancer drug development. We previously identified lead compounds that inhibited both Hsp27 and tubulin. These compounds exhibited extensive anti-cancer activities against the proliferation of various human cancer cell lines. In the current study, a systematic ligand based structural optimization led to new analogs that significantly inhibited the growth of a panel of breast cancer cell lines. Furthermore, the most potent compounds were examined with tubulin polymerization assay and Hsp27 chaperone activity assay. The compounds showed potent tubulin polymerization inhibition but no Hsp27 inhibitory effect. The structural optimization dissected the dual activity and improved the selectivity of the compounds for tubulin. The results revealed several structural moieties of the lead compounds that are critical for Hsp27 inhibition. The modification of these structural fragments eliminated Hsp27 inhibition, but did not harm tubulin-targeting effects of the compounds. This result further defined the structureeactivity relationship between the tubulin and Hsp27 effects of these compounds.

Comments

This research was supported by a startup fund from Cleveland State University, and also partially supported by grant R15AI 103889 (B. Su), Center for Gene Regulation in Health and Disease (GRHD) of Cleveland State University and Ohio Department of Development (ODOD) and National Science Foundation Major Research Instrumentation Grants (CHE-0923398 and CHE-1126384).

DOI

10.1016/j.ejmech.2014.04.038

Version

Postprint

Volume

80

Share

COinS