ustiloxin-b has been researched along with rhizoxin* in 1 studies
1 other study(ies) available for ustiloxin-b and rhizoxin
Article | Year |
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Ustiloxins, new antimitotic cyclic peptides: interaction with porcine brain tubulin.
Biochemical and electron microscopic studies demonstrated that ustiloxins A-D, which are antimitotic 13-membered cyclic peptides produced by the rice plant pathogen Ustilaginoidea virens, strongly inhibited the polymerization of porcine brain tubulin in vitro and depolymerized pre-formed microtubules. The IC50 values of polymerization inhibited by ustiloxins A-D were determined to be 0.7, 2.8, 4.4 and 6.6 microM, respectively, under the experimental conditions used, indicating that ustiloxin A is the most potent inhibitor of tubulin polymerization currently known. Ustiloxins A-C were found to inhibit the binding of radiolabelled rhizoxin to tubulin with inhibition constants (Ki) of 0.08, 0.13 and 0.23 microM, respectively, and also inhibited the binding of radiolabelled phomopsin A as strongly as rhizoxin. These results suggest that the binding site of ustiloxins is identical with that of rhizoxin. Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Binding Sites; Brain; Dose-Response Relationship, Drug; Lactones; Macrolides; Molecular Sequence Data; Mycotoxins; Peptides; Peptides, Cyclic; Swine; Tubulin | 1995 |