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Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties.

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SASSE, FLORENZ, SIEINMETZ, HEINRICH, HEIL, JÜRGEN, HÖFLE, GERHARD, REICHENBACH, HANS·2000·The Journal of Antibiotics

Abstract

New cytostatic compounds, tubulysins, were isolated from the culture broth of strains of the myxobacteria Archangium gephyra and Angiococcus disciformis. The compounds are peptides partly consisting of unusual amino acids and are distantly related to the dolastatins. The tubulysins were not active against bacteria and only little against fungi, but showed high cytostatic activity against mammalian cell lines with IC50 values in the picomolar range. An incubation with 50 ng/ml tubulysin A led to a complete disappearance of the microtubuli network of the cells within 24 hours. The more active tubulysin D induced multipolar spindles: At 0.5 ng/ml all mitotic cells showed more than four spindle poles.

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Metadata

Authors
SASSE, F., SIEINMETZ, H., HEIL, J., HÖFLE, G., & REICHENBACH, H.
Venue
The Journal of Antibiotics
Published
2000
Volume
53
Issue
9
Pages
879-885
ISSN
  • 0021-8820 (ISSN-L)
  • 1881-1469
OpenAlex
W1985072203
Cited by
257
References
0
FWCI
2.27
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties. https://app.cochat.ai/papers/10.7164/antibiotics.53.879
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SASSE, F., SIEINMETZ, H., HEIL, J., HÖFLE, G., & REICHENBACH, H. (2000). Tubulysins, New Cytostatic Peptides from Myxobacteria Acting on Microtubuli. Production, Isolation, Physico-chemical and Biological Properties. The Journal of Antibiotics. https://doi.org/10.7164/antibiotics.53.879

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.