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Abstract
Colchiceine, a closely related structural analog of colchicine possessing a C-ring tropolone, has been shown to be a potent inhibitor of microtubule assembly in vitro (I 50 = 20 μM). The mechanism of inhibition is mediated through binding to tubulin ( K A = 1.2 ± 0.7 × 10 4 M −1), although potentially not through the colchicine receptor site. Supporting the hypothesis of an alternate receptor are the observation of colchiceine binding to the isolated colchicine-tubulin complex ( K A = 2.2 ± 1.0 × 10 4 M −1), the poor correlation between the competitive inhibition of colchicine binding ( K l = 125 μM) and the inhibition of microtubule assembly, and different structure-activity relationships for colchiceine analogs as compared to the colchicine series.
Published Version
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