Binding of colchicine to purified microtubule protein.

Kinetics of Colchicine Binding to Purified &Tubulin Isotypes from Bovine Brain*

Tubulin, the constituent protein of microtubules, is an a@ heterodimer; both a and B exist in several isotypic forms whose functional significance is not precisely known. The antimitotic alkaloid colchicine binds to mammalian brain tubulin in a biphasic manner under pseudo-first-order conditions in the presence of a large excess of colchicine (Garland, D. L. (1978) Biochernis try 17, 4266-4272)...

Binding of dihydroxynaphthyl aryl ketones to tubulin colchicine site inhibits microtubule assembly.

Dihydroxynaphthyl aryl ketones 1-5 have been evaluated for their abilities to inhibit microtubule assembly and the binding to tubulin. Compounds 3, 4 and 5 displayed competitive inhibition against colchicine binding, and docking analysis showed that they bind to the tubulin colchicine-binding pocket inducing sheets instead of microtubules. Remarkable differences in biological activity observed ...

Competitive inhibition of colchicine binding to tubulin by microtubule-associated proteins.

Microtubule-associated proteins (MAPs) promote tubulin polymerization, whereas colchicine inhibits this process. In this paper, MAPs have been shown to inhibit colchicine binding to tubulin in a competitive manner. Attempts were made to identify which of the MAPs fraction(s) was responsible; both tau protein (a thermostable molecule with a molecular weight of approximately 70,000) and a high mo...

Interaction of colchicine analogues with purified tubulin.

Binding of two colchicine analogues, desacetamidocolchicine and 2-methoxy-5-(2',3',4'-trimethoxyphenyl) tropone to purified tubulin have been studied. Both analogues bind to tubulin with a significant increase in fluorescence polarization of the drugs in solutions containing tubulin. The Kd for tubulin-drug complexes were found to be 1.25 X 10(-6) M and 1.08 X 10(-6) M for desacetamidocolchicin...

structure activity relationship (sar) investigation on the binding properties of ligands similar to combretastatin to colchicine binding site of tubulin protein as anti-cancer drug