Interaction of epothilone analogs with the paclitaxel binding site: relationship between binding affinity, microtubule stabilization, and cytotoxicity

Chem Biol. 2004 Feb;11(2):225-36. doi: 10.1016/j.chembiol.2004.01.014.

Abstract

The interactions of epothilone analogs with the paclitaxel binding site of microtubules were studied. The influence of chemical modifications in the C15 side chain and in C12 on binding affinity and microtubule elongation was characterized. Modifications favorable for binding affinity are (1). a thiomethyl group at C21 of the thiazole side chain, (2). a methyl group at C12 in S configuration, (3). a pyridine side chain with C15 in S configuration, and (4). a cyclopropyl moiety between C12 and C13. The same modification in different ligands has similar effect on affinity, allowing good structure-affinity characterization. The correlation between binding, microtubule stabilization, and cytotoxicity of the compounds has been determined, showing differential effects of the modifications. The binding constants correlate well with IC(50) values, demonstrating that affinity measurements are a useful tool for drug design.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / metabolism
  • Antineoplastic Agents / toxicity*
  • Binding Sites
  • Cell Line, Tumor
  • Drug Design
  • Epothilones / chemistry*
  • Epothilones / metabolism
  • Epothilones / toxicity*
  • Female
  • Humans
  • Microtubules / chemistry
  • Microtubules / drug effects*
  • Molecular Conformation
  • Paclitaxel / metabolism*
  • Structure-Activity Relationship
  • Thermodynamics

Substances

  • Antineoplastic Agents
  • Epothilones
  • Paclitaxel