Hemiasterlin and Dolastatin 10 Bind the Vinca-Peptide Site Of Tubulin

Fluorescence Analyses Indicate That Hemiasterlin & Dolastatin 10 Bind the Vinca/Peptide Site Of Tubulin
The binding of vinca site agents to tubulin results in fluorescence quenching of ~ 3 surface-exposed tryptophans in tubulin, whether the agents induce tubulin oligomers (e.g., vinblastine) or not (e.g., maytansine, rhizoxin). Colchicine-site agents do not have this quenching effect [Biochem 34: 7010-7019, 1995].
Hemiasterlin and dolastatin 10, like other vinca site binding agents, quench the fluorescence emission of more than one tryptophan in tubulin.
Hemiasterlin inhibits the binding to tubulin of radioactive vinblastine, dolastatin 10, and GTP (data not shown here).

Thus hemiasterlin and dolastatin 10 bind to the vinca / peptide region of tubulin.

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