Two New Ring-Contracted Congeners of Rhizopodin Illustrate Significance of the Ring Moiety of Macrolide Toxins on the Actin Disassembly-Mediated Cytotoxicity

DOI Web Site Web Site PubMed 参考文献4件
  • Oku Naoya
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • Matsumoto Ayaka
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • Matsunaga Takayuki
    Toyama Prefectural Institute for Pharmaceutical Research
  • Asano Yuhki
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • Kasai Hiroaki
    Kamaishi Laboratory, Kitasato University
  • Matoba Shouhei
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • Igarashi Yasuhiro
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University

この論文をさがす

抄録

Two new cytotoxic dilactones, bisisorhizopodin (1) and isorhizopodin (2), together with known divalent actin depolymerizer rhizopodin (3), were isolated from the culture broth of a myxobacterium Myxococcus stipitatus. Spectroscopic analyses established that 1 and 2 are doubly and singly acyl-migrated isomers of 3, respectively, and comparison of their cytotoxicity revealed gradual decrease in the activity as the size of the ring contracted. Because the side chains of macrolide toxins uniformly block the contact between the actin protomers, the present result demonstrates substantial contribution of structurally diverse rings to the affinity of macrolide toxins for its target protein.

収録刊行物

参考文献 (4)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ