ReviewMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents2026
Flavonoids as colchicine binding site inhibitors: emerging scaffolds in anticancer drug design.
Review in Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Tubulin inhibition remains a well-established strategy in anticancer therapy, mediated primarily through three binding sites on the α-β tubulin heterodimers: taxane, vinca, and colchicine binding site (CBS). Although several clinically approved drugs target the taxane and vinca sites, their efficacy is often compromised by multidrug resistance. In contrast, CBS remains an underexploited yet highly promising target, as no anticancer drug has been approved that specifically binds this site. Flavonoids, a diverse class of naturally occurring polyphenols, share structural features with colchicine and have emerged as potential CBS inhibitors with favourite safety profiles. Reported tubulin-inhibiting flavonoids encompass polymethoxylated (PMF), polyhydroxylated (PHF), and synthetic or semi-synthetic derivatives, with the most potent compounds exhibiting sub micromolar IC
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