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

作者信息

Toki S, Agatsuma T, Ochiai K, Saitoh Y, Ando K, Nakanishi S, Lokker N A, Giese N A, Matsuda Y

机构信息

Tokyo Research Laboratories, Kyowa Hakko Kogyo Co, Ltd, Japan.

出版信息

J Antibiot (Tokyo). 2001 May;54(5):405-14. doi: 10.7164/antibiotics.54.405.

DOI:10.7164/antibiotics.54.405
PMID:11480883
Abstract

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 through the inhibition of PDGF BB binding to the PDGF beta-receptor.

摘要

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