Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B

Pharmacol Ther. 1992;55(1):31-51. doi: 10.1016/0163-7258(92)90028-x.

Abstract

This paper summarizes published data on the interactions of tubulin with antimitotic compounds that inhibit the binding of vinca alkaloids to the protein. These are all relatively complex natural products isolated from higher plants, fungi and marine invertebrate animals. These agents are maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B and their congeners. Effects on tubulin polymerization, ligand binding interactions and structure-activity relationships are emphasized.

Publication types

  • Review

MeSH terms

  • Animals
  • Antibiotics, Antineoplastic / pharmacology
  • Antineoplastic Agents / pharmacology*
  • Depsipeptides*
  • Ethers, Cyclic / pharmacology
  • Lactones / pharmacology
  • Macrolides
  • Maytansine / pharmacology
  • Mycotoxins / pharmacology
  • Oligopeptides / pharmacology
  • Tubulin / drug effects*
  • Tubulin / metabolism
  • Vinca Alkaloids / metabolism
  • Vinca Alkaloids / pharmacology*

Substances

  • Antibiotics, Antineoplastic
  • Antineoplastic Agents
  • Depsipeptides
  • Ethers, Cyclic
  • Lactones
  • Macrolides
  • Mycotoxins
  • Oligopeptides
  • Tubulin
  • Vinca Alkaloids
  • dolastatin 15
  • Maytansine
  • halichondrin B
  • phomopsin
  • rhizoxin
  • dolastatin 10