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

Cheng Zhu Wu, An Na Moon, Oksik Choi, Sun Young Kang, Jung Joon Lee, Dongho Lee, Bang Yeon Hwang, Young Ho Kim, Hong Sub Lee, Young Soo Hong

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1997-2001
Number of pages5
JournalArchives of Pharmacal Research
Issue number12
StatePublished - Dec 2010

Bibliographical note

Funding Information:
This work was supported by the 21C Frontier Microbial Genomics and Application Center, the Ministry of Science and Technology, Republic of Korea and by a grant from KRIBB Research Initiative Program.


  • ATPase inhibitor
  • Hsp90 inhibitor
  • Salaceyin
  • Streptomyces


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