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Discovery of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl)acetates as potent Hsp90 inhibitors with selectivity over TRAP1

  • 주제(키워드) Hsp90 , TRAP1 , Grp94 , Inhibitor , Selectivity , Resorcinol , Triazole
  • 주제(기타) Chemistry, Medicinal; Chemistry, Organic
  • 설명문(일반) [Jung, Sejin; Kim, Darong; Lee, Won Seok; Hong, Ki Bum; Lee, Ji Hoon] DGMIF, New Drug Dev Ctr, Daegu 41061, South Korea; [Yoon, Nam Gu; Lee, Changwook; Kang, Byoung Heon] UNIST, Dept Biol Sci, Ulsan 44919, South Korea; [Yang, Sujae; Kang, Soosung] Ewha Womans Univ, Coll Pharm, Seoul 03760, South Korea; [Yang, Sujae; Kang, Soosung] Ewha Womans Univ, Grad Sch Pharmaceut Sci, Seoul 03760, South Korea; [Kang, Soosung] Korea Basic Sci Inst, Western Seoul Ctr, Seoul 03760, South Korea
  • 등재 SCIE, SCOPUS
  • 발행기관 PERGAMON-ELSEVIER SCIENCE LTD
  • 발행년도 2020
  • 총서유형 Journal
  • URI http://www.dcollection.net/handler/ewha/000000165908
  • 본문언어 영어
  • Published As http://dx.doi.org/10.1016/j.bmcl.2019.126809
  • PubMed https://pubmed.ncbi.nlm.nih.gov/31839539

초록/요약

As the most abundant heat shock protein (HSP), Hsp90 is actively involved in tumor cell growth and various responses to anti-carcinogenic stress. Hsp90 has thus emerged as a potential drug target. A structure-based drug design approach was applied to develop novel resorcinolyltriazole derivatives as Hsp90 inhibitors. Structure-activity relationships (SARs) and molecular docking were investigated to provide a rationale for binding affinity and paralog selectivity. Click chemistry between iodoethynylresorcinol and an azido derivative was used to synthesize a new family of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl) acetates that exhibited Hsp90 binding affinities of 40-100 nM (IC50). Among the synthesized molecules, the triazole alkyl acetates displayed the highest Hsp90 binding affinities. Their potency against Hsp90 was over 100-fold stronger than against TRAP1 and 1-3-fold stronger than against Grp94. In particular, compounds 18, 19, and 30 had Hsp90 inhibitory activities of similar to 45 nM (IC50) and they displayed over 350-fold selectivity for Hsp90 over TRAP1.

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