Background: A number of chemically diverse substances bind to the tubulin and inhibit
cell proliferation by disrupting microtubule dynamics. There are four binding sites for the ligands
binding to the tubulin; taxane/epothilone and laulimalide/peloruside binding ligands stabilize microtubule
while vinca and colchicine binding site agents promote microtubule depolymerization. Most
of the tubulin binding ligands disturb the tubulin-microtubule dynamic equilibrium but these may
exhibit anticancer activities through different mechanisms. Taxanes and epothilones are widely used
cytotoxic agents and are found effective against different types of human malignancies. However,
taxanes are susceptible to pgp mediated multi-drug resistance, dose limiting hematopoietic toxicity
and cumulative neurotoxicity. Vinca alkaloids are already in clinical practice, but ligands binding to
the colchicine site are still in the different stages of clinical trials.
Objective: In the current review article, plausible mechanistic details about the interactions of ligands
at the binding pocket and subsequent changes in the tubulin structure are described. The review
article also illustrated different formulations of the tubulin binding agents in combination with other
chemotherapeutic agents and their therapeutic potential against various human malignancies.
Conclusion: Tubulin targeting agents emerged as one of the most successful anticancer drugs and a
number of structurally different chemical compounds are in advance stages of clinical development.