RP-1776, a novel cyclic peptide produced by Streptomyces sp., inhibits the binding of PDGF to the extracellular domain of its receptor.

@article{Toki2001RP1776AN,
  title={RP-1776, a novel cyclic peptide produced by Streptomyces sp., inhibits the binding of PDGF to the extracellular domain of its receptor.},
  author={Shinichiro Toki and Tsutomu Agatsuma and Keiko Ochiai and Yutaka Saitoh and Katsuhiko Ando and Satoshi Nakanishi and Nathalie Andrienne Lokker and Neill A. Giese and Yuzuru Matsuda},
  journal={The Journal of antibiotics},
  year={2001},
  volume={54 5},
  pages={
          405-14
        }
}
RP-1776, a novel cyclic peptide, was isolated from the culture broth of Streptomyces sp. KY11784. RP-1776 selectively inhibited the binding of PDGF BB to the extracellular domain of the PDGF beta-receptor with an IC50 value of 11 +/- 6 microM. Detailed binding experiments suggested that RP-1776 directly interacts with PDGF BB. RP-1776 inhibited the phosphorylation of the PDGF beta-receptor induced by PDGF BB. These results suggested that RP-1776 antagonizes the signaling of PDGF BB probably… 
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