Tubulin binding properties of two chiral isomers with 1-deaza-7,8-dihydropteridine structure.

  title={Tubulin binding properties of two chiral isomers with 1-deaza-7,8-dihydropteridine structure.},
  author={D. Leynadier and V. Peyrot and M. Sarrazin and J. Andreu and C. Temple and G. Rener and C. Briand},
  journal={Advances in experimental medicine and biology},
It has been shown that ethyl 5-amino-l,2-dihydro-2-methyl-3-phenyl pyrido (3,4-b)pyrazin-7-yl carbamate (NSC 370147) inhibits microtubule formation, that this racemic compound binds to tubulin at or near the colchicine site, and that it enhances the binding of Vincristine to tubulin1. It appeared of interest to evaluate the activity of the R-enantiomer (NSC 613863) and the S-enantiomer (NSC 613862, CI 980). Hence, their interactions were examined at molecular level. Furthermore, we compared the… Expand


Interaction of tubulin with bifunctional colchicine analogues: an equilibrium study.
Excess analogue concentration under microtubule-promoting conditions induces an abnormal cooperative polymerization of tubulin, similar to that of the tubulin-colchicine complex. Expand
Comparison of 1,2-dihydropyrido[3,4-b]pyrazines (1-deaza-7,8-dihydropteridines) with several other inhibitors of mitosis.
Emphasis in further testing was placed upon NSC 370147, because it is easier to synthesize and is more stable than some of the other compounds of this type and because its greater solubility in water facilitates its formulation for therapeutic administration. Expand
Podophyllotoxin as a probe for the colchicine binding site of tubulin.
It is concluded that both podophyllotoxin and colchicine each have at least two points of attachment to tubulin and that they share one of them, the binding region of the trimethoxyphenyl moiety. Expand
Action of the vinca alkaloids vincristine, vinblastine, and desacetyl vinblastine amide on microtubules in vitro.
The differential actions of vinblastine, vincristine, and desacetyl v inblastine amide in vivo seems to be based on some biological process other than the reaction with tubulin or the microtubules per se. Expand
Effect of antimitotic drugs on tubulin GTPase activity and self-assembly.
The colchicine-stimulated GTPase activity of tubulin appears to be due to the tubulin, suggesting a selective action of vinblastine on the early stages of the polymerization reaction. Expand