A tripeptide derived from marine sponges (among them Hemiasterella minor) that will block polymerization of microtubules by binding to the vinca-alkaloid binding site on β-tubulin. The amino acids are unusual, and synthetic derivatives of hemiasterlin have been produced for chemotherapeutic use. In standard tubulin polymerization assays it is more potent than vincristine, marginally less active than dolastatin-10, and approximately equal in activity to cryptophycin-1. See phomopsin A.
Subjects: Medicine and Health.