Chloroacetates of 2- and 3-demethylthiocolchicine: specific covalent interactions with tubulin with preferential labeling of the beta-subunit

Biochem Biophys Res Commun. 1992 Sep 30;187(3):1350-8. doi: 10.1016/0006-291x(92)90451-p.

Abstract

We synthesized two chemically reactive A ring modified analogs of colchicine, 2-chloroacetyl-2-demethylthiocolchicine (2-CTC) and 3-chloroacetyl-3-demethylthiocolchicine (3-CTC). Both are similar to colchicine as inhibitors of tubulin polymerization and act as competitive inhibitors of colchicine binding (apparent Ki values, 3 microM). [14C]-labeled 2-CTC and 3-CTC bound to tubulin at 37 degrees C but not at 0 degree C, and bound drug formed covalent bond(s) with tubulin. The binding and covalent reactions were inhibited by podophyllotoxin. About 60% of the bound 3-CTC rapidly formed a covalent bond with tubulin. With 2-CTC the covalent reaction was slower than the binding reaction, and only one-third of the bound 2-CTC reacted covalently with tubulin. The ratio of radiolabel in beta-tubulin to that in alpha-tubulin was about 4:1 with both 2-CTC and 3-CTC.

MeSH terms

  • Binding, Competitive
  • Colchicine / analogs & derivatives*
  • Colchicine / chemistry
  • In Vitro Techniques
  • Structure-Activity Relationship
  • Tubulin / chemistry*

Substances

  • Tubulin
  • 3-chloroacetyl-3-demethylthiocolchicine
  • 2-chloroacetyl-2-demethylthiocolchicine
  • Colchicine