Direct photoaffinity labeling by dolastatin 10 of the amino-terminal peptide of beta-tubulin containing cysteine 12.

@article{Bai2004DirectPL,
  title={Direct photoaffinity labeling by dolastatin 10 of the amino-terminal peptide of beta-tubulin containing cysteine 12.},
  author={Ruoli Bai and David G. Covell and G. F. Taylor and John A Kepler and Terry D. Copeland and Nga Yen Nguyen and George R. Pettit and Ernest Hamel},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 29},
  pages={30731-40}
}
Tubulin with bound [5-3H]dolastatin 10 was exposed to ultraviolet light, and 8-10% of the bound drug cross-linked to the protein, most of it specifically. The primary cross-link was to the peptide spanning amino acid residues 2-31 of beta-tubulin, but the specific amino acid could not be identified. Indirect studies indicated that cross-link formation occurred between cysteine 12 and the thiazole moiety of dolastatin 10. An equipotent analog of dolastatin 10, lacking the thiazole ring, did not… CONTINUE READING