Chloropeptins, New Anti-HIV Antibiotics Inhibiting gp120-CD4 Binding from Streptomyces sp. I. Taxonomy, Fermentation, Isolation, and Physico-chemical Properties and Biological Activities.
- 1 January 1997
- journal article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 50 (1) , 58-65
- https://doi.org/10.7164/antibiotics.50.58
Abstract
Chloropeptins I and II, which are gp120-CD4 binding inhibitors, were isolated as pale yellow-brown powders from the mycelia of a soil actinomycete, Streptomyces sp, WK-3419. Their physico-chemical properties showed that they are chlorinated peptides. Chloropeptin I (C61H45N7O15Cl6) is a novel compound, but chloropeptin II was identified as complestatin. Both compounds inhibited gp120-CD4 binding (IC50: 1.3 and 2.0 microM, respectively), the cytopathic effect of HIV in MT-4 cells (EC50: 1.6 and 1.7 microM, respectively) and syncytium formation in co-cultured HIV-1-infected and uninfected MOLT-4 cells (IC50. 0.5 and 1.1 microM, respectively). Chloropeptin I was synergistic in the inhibition of the cytopathic effect when combined with other anti-HIV drugs such as zidovudine (AZT), didanosine (ddI), zalcitabine (ddC) and nevirapine.Keywords
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