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KMID : 0043320100330121997
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Archives of Pharmacal Research
2010 Volume.33 No. 12 p.1997 ~ p.2001
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6-alkylsalicylic acid analogues inhibit in vitro ATPase activity of heat shock protein 90
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Wu Cheng Zhu
Moon An-Na
Choi Ok-Sik
Kang Sun-Young
Lee Jung-Joon
Lee Dong-Ho
Hwang Bang-Yeon
Kim Young-Ho
Lee Hong-Sub
Hong Young-Soo
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Abstract
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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.
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KEYWORD
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Salaceyin, ATPase inhibitor, Hsp90 inhibitor, Streptomyces
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