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Chemical Compound Review

Hemiasterlin     (E,4S)-4-[[(2S)-3,3-dimethyl- 2-[[(2S)-3...

Synonyms: Milnamide B, SureCN57313, CHEMBL185151, NSC-695242, NSC695242, ...
 
 
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Disease relevance of Hemiasterlin

  • The basis of resistance to a synthetic analogue of hemiasterlin, HTI-286 (HTI), was examined in cell populations derived from ovarian carcinoma (A2780/1A9) cells selected in HTI-286 [1].
 

High impact information on Hemiasterlin

  • Hemiasterlin is a potent antimitotic peptide that interferes with microtubule dynamics at picomolar concentrations in cell culture [2].
  • HTI-286, a synthetic analogue of the tripeptide hemiasterlin, is a potent antimicrotubule agent that circumvents P-glycoprotein-mediated resistance in vitro and in vivo [3].
  • Hemiasterlin is a natural product derived from marine sponges that, like other structurally diverse peptide-like molecules, binds to the Vinca-peptide site in tubulin, disrupts normal microtubule dynamics, and, at stoichiometric amounts, depolymerizes microtubules [3].
  • A synthetic analogue of the tripeptide hemiasterlin, designated HTI-286, depolymerizes microtubules, is a poor substrate for P-glycoprotein, and inhibits the growth of paclitaxel-resistant tumors in xenograft models [4].
  • Two photoaffinity analogues of the tripeptide, hemiasterlin, exclusively label alpha-tubulin [4].
 

Biological context of Hemiasterlin

 

Anatomical context of Hemiasterlin

  • Modifications of the D-piece carboxylic acid group of the hemiasterlin analog HTI-286 gave tubulin inhibitors which were potent cytotoxic agents in taxol resistant cell lines expressing P-glycoprotein [7].
 

Associations of Hemiasterlin with other chemical compounds

  • Fluorescence correlation spectroscopy (FCS) was applied to investigate the stability of tubulin rings that result from the interaction of alpha beta-tubulin dimers with three vinca domain-binding peptides--cryptophycin 1, hemiasterlin, and dolastatin 10 [8].
  • Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: comparison with dolastatin 10 and cryptophycin 1 [9].
  • The conformation of HTI-286 (I) in complex with the protein was determined from TRNOESY/ROESY experiments and is similar to the X-ray crystal structure conformation observed for hemiasterlin methyl ester in the absence of protein [10].
 

Analytical, diagnostic and therapeutic context of Hemiasterlin

References

  1. Tumor cells resistant to a microtubule-depolymerizing hemiasterlin analogue, HTI-286, have mutations in alpha- or beta-tubulin and increased microtubule stability. Poruchynsky, M.S., Kim, J.H., Nogales, E., Annable, T., Loganzo, F., Greenberger, L.M., Sackett, D.L., Fojo, T. Biochemistry (2004) [Pubmed]
  2. A missense mutation in Caenorhabditis elegans prohibitin 2 confers an atypical multidrug resistance. Zubovych, I., Doundoulakis, T., Harran, P.G., Roth, M.G. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. HTI-286, a synthetic analogue of the tripeptide hemiasterlin, is a potent antimicrotubule agent that circumvents P-glycoprotein-mediated resistance in vitro and in vivo. Loganzo, F., Discafani, C.M., Annable, T., Beyer, C., Musto, S., Hari, M., Tan, X., Hardy, C., Hernandez, R., Baxter, M., Singanallore, T., Khafizova, G., Poruchynsky, M.S., Fojo, T., Nieman, J.A., Ayral-Kaloustian, S., Zask, A., Andersen, R.J., Greenberger, L.M. Cancer Res. (2003) [Pubmed]
  4. Two photoaffinity analogues of the tripeptide, hemiasterlin, exclusively label alpha-tubulin. Nunes, M., Kaplan, J., Wooters, J., Hari, M., Minnick, A.A., May, M.K., Shi, C., Musto, S., Beyer, C., Krishnamurthy, G., Qiu, Y., Loganzo, F., Ayral-Kaloustian, S., Zask, A., Greenberger, L.M. Biochemistry (2005) [Pubmed]
  5. Structure-based identification of the binding site for the hemiasterlin analogue HTI-286 on tubulin. Ravi, M., Zask, A., Rush, T.S. Biochemistry (2005) [Pubmed]
  6. Inhibition of hepatic tumor cell proliferation in vitro and tumor growth in vivo by taltobulin, a synthetic analogue of the tripeptide hemiasterlin. Vashist, Y.K., Tiffon, C., Stoupis, C., Redaelli, C.A. World J. Gastroenterol. (2006) [Pubmed]
  7. D-piece modifications of the hemiasterlin analog HTI-286 produce potent tubulin inhibitors. Zask, A., Birnberg, G., Cheung, K., Kaplan, J., Niu, C., Norton, E., Yamashita, A., Beyer, C., Krishnamurthy, G., Greenberger, L.M., Loganzo, F., Ayral-Kaloustian, S. Bioorg. Med. Chem. Lett. (2004) [Pubmed]
  8. Stability of drug-induced tubulin rings by fluorescence correlation spectroscopy. Boukari, H., Nossal, R., Sackett, D.L. Biochemistry (2003) [Pubmed]
  9. Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: comparison with dolastatin 10 and cryptophycin 1. Bai, R., Durso, N.A., Sackett, D.L., Hamel, E. Biochemistry (1999) [Pubmed]
  10. Mapping the bound conformation and protein interactions of microtubule destabilizing peptides by STD-NMR spectroscopy. Milton, M.J., Thomas Williamson, R., Koehn, F.E. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
  11. Hybrids of the hemiasterlin analogue taltobulin and the dolastatins are potent antimicrotubule agents. Zask, A., Kaplan, J., Musto, S., Loganzo, F. J. Am. Chem. Soc. (2005) [Pubmed]
 
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