• Title/Summary/Keyword: Cyclo(L-tryptophanyl-L-tryptophanyl)

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Identification of Streptomyces sp. KH29, Which Produces an Antibiotic Substance Processing an Inhibitory Activity Against Multidrug-Resistant Acinetobacter baumannii

  • Lee, Keyong-Ho;Kim, Gye-Woong;Rhee, Ki-Hyeong
    • Journal of Microbiology and Biotechnology
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    • v.20 no.12
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    • pp.1672-1676
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    • 2010
  • The Actinomycete strain KH29 is antagonistic to the multidrug-resistant Acinetobacter baumannii. Based on the diaminopimelic acid (DAP) type, and the morphological and physiological characteristics observed through the use of scanning electron microscopy (SEM), KH29 was confirmed as belonging to the genus Streptomyces. By way of its noted 16S rDNA nucleotide sequences, KH29 was found to have a relationship with Streptomyces cinnamonensis. The production of an antibiotic from this strain was found to be most favorable when cultured with glucose, polypeptone, and yeast extract (PY) medium for 6 days at $27^{\circ}C$. The antibiotic produced was identified, through comparisons with reported spectral data including MS and NMR as a cyclo(L-tryptophanyl-L-tryptophanyl). Cyclo(L-Trp-L-Trp), from the PY cultures of KH29, was seen to be highly effective against 41 of 49 multidrug-resistant Acinetobacter baumannii. Furthermore, cyclo(L-Trp-L-Trp) had antimicrobial activity against Bacillus subtilis, Micrococcus luteus, Staphylococcus aureus, Saccharomyces cerevisiae, Aspergillus niger, and Candida albicans, However, it was ineffective against Streptomyces murinus.

Proteome Analysis of Apicidin- Treated Human Cervix Cancer Cells

  • Shim , Won-Jo;Cho, Eun-jung;Lee, Hoi-Young;Hong , Sung-Youl;Han, Jeung-Whan;Lee, Hyang-Woo
    • Proceedings of the PSK Conference
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    • 2002.10a
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    • pp.323.1-323.1
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    • 2002
  • Apicidin [cyclo(N-O-methyl-l -tryptophanyl-L -isoleucinyl-D-pipecolinyl-L-2-amino-8-oxodecano y)]. a histone deacetylase inhibitor. has been shown to cause growth arrest and morphological change of cancer cells. resulting from the alternation of protein expression. such as p21WAF1/Cip1 and gelsolin. However. proteome of altered by apicidin are poorly studied. In this study. we used a functional proteornics approach to identify the proteome altered by apicidin in Hela cells at 24hr post-treatment. (omitted)

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