Interaction of dolastatin 10 with bovine brain tubulin

Richard F. Luduena, Mary Carmen Roach, Veena Prasad, George Pettit

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

Dolastatin 10 is an unusual peptide of marine origin which binds to tubulin in the vinblastine/ maytansine/phomopsin-binding region and potently inhibits mitosis. Using N, N′-ethylenebis(iodoacetamide) (EBI) and iodo[14C]acetamide as probes for the effects of ligands on the thiol groups of tubulin, we found that dolastatin 10 has effects on the sulfhydryls indistinguishable from those of phomopsin A but quite different from those of vinblastine and maytansine. Using the binding of bis-5,5'-[8-(N-phenyl) aminonaphthalene-1-sulfonic acid](BisANS) as a measure of tubulin decay, we found that dolastatin 10 resembled phomopsin A in that decay was not detectable by this assay in its presence. Interestingly, both otherwise very different peptides are among the most effective inhibitors of tubulin decay yet discovered.

Original languageEnglish (US)
Pages (from-to)539-543
Number of pages5
JournalBiochemical Pharmacology
Volume43
Issue number3
DOIs
StatePublished - Feb 4 1992

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

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