Inhibition of [3H]mebendazole binding to tubulin by structurally diverse microtubule inhibitors which interact at the colchicine binding site.
A rapid and convenient radioligand assay was used to characterise the interaction of several structurally diverse microtubule inhibitors with the colchicine binding domain of tubulin. Values determined for the inhibition of [3H]mebendazole binding to tubulin by colchicine, combretastatin A4, NSC 181928, NSC 321567, podophyllotoxin and tubulozole-C provided an independent measure of the relative potency of these compounds. This methodology has several advantages over the inhibition of [3H]colchicine binding as a technique for investigating the molecular mechanisms involved in determining tubulin-ligand interactions.
D000818:Animals; D001665:Binding Sites; D003078:Colchicine / Q000378:metabolism*; D008463:Mebendazole / Q000378:metabolism*; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D011485:Protein Binding; D011869:Radioligand Assay; D012756:Sheep; D014316:Tritium; D014404:Tubulin / Q000378:metabolism*
D014404:Tubulin; D014316:Tritium; D008463:Mebendazole; D003078:Colchicine