6-alkylsalicylic acid analogues inhibit In vitro ATPase activity of heat shock protein 90

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6-alkylsalicylic acid analogues inhibit In vitro ATPase activity of heat shock protein 90
C Z Wu; A N Moon; Oksic Choi; Sun-Young Kang; Jung Joon Lee; D Lee; B Y Hwang; Y H Kim; H S Lee; Young-Soo Hong
Bibliographic Citation
Archives of Pharmacal Research, vol. 33, no. 12, pp. 1997-2001
Publication Year
The molecular chaperone heat shock protein 90 (Hsp90) is responsible for maintaining the correct folding and stability of many signaling proteins. It is a promising target of cancer therapeutics and several other diseases, including neurodegenerative disease, nerve injuries, inflammation, and infection. In an effort to identify new Hsp90 inhibitors from natural sources using an in vitro ATPase inhibition assay, two 6-alkylsalicylic acid analogues, salaceyin A and B were identified from the culture extract of Streptomyces. Salaceyin A and B exhibited moderate ATPase inhibitory activities with IC50 values of 68.3 and 65.2 μM, respectively. Binding of salaceyins to human Hsp90α was examined by competition binding experiments with ATP-Sepharose beads. However, the compounds exhibited no degradation activity of Hsp90 client proteins, Her2, c-Raf, or Akt. ⓒ 2010 The Pharmaceutical Society of Korea and Springer Netherlands.
SalaceyinATPase inhibitorHsp90 inhibitorStreptomyces
Pharmaceutical Soc Korea
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Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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