Experimental and computational study of the interaction of novel colchicinoids with a recombinant human αI/βI-tubulin heterodimer

Chem Biol Drug Des. 2013 Jul;82(1):60-70. doi: 10.1111/cbdd.12132.

Abstract

The binding free energies on human tubulin of selected colchicine and thiocolchicine compounds were determined. Two methods were used for the determination of binding free energies: one is based on theoretical prediction simulating the dissociation of the compound from tubulin using a series of molecular dynamics simulations, and the other method involves a series of experiments that measured the affinity of the compound on a synthetically expressed and purified tubulin protein using a spectrofluorometric technique.

MeSH terms

  • Binding Sites
  • Colchicine / chemistry*
  • Colchicine / metabolism
  • Dimerization
  • Humans
  • Kinetics
  • Molecular Docking Simulation
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Spectrometry, Fluorescence
  • Thermodynamics
  • Tubulin / chemistry*
  • Tubulin / genetics
  • Tubulin / metabolism

Substances

  • Recombinant Proteins
  • Tubulin
  • Colchicine