Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 23, Issue 23, Pages 6427-6431Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2013.09.050
Keywords
Hsp90; Structure-based design; Cancer; Molecular docking; Triazines
Categories
Funding
- National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [2011-0023605]
- College of Pharmacy (institute for new drug development) of Keimyung University
- National Research Foundation of Korea [2011-0023605] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in regulating the maturation and stabilization of many oncogenic proteins. In an attempt to discover a new class of Hsp90 inhibitors, a series of 1,3,5-triazine compounds were rationally designed, synthesized, and their biological activities were evaluated. Compound 3b was found to degrade Hsp90's client proteins of Her2, Met and Akt and to induce the expression level of Hsp70. The binding mode of 3b in the ATP-binding site of Hsp90 was predicted by the molecular docking. (C) 2013 Elsevier Ltd. All rights reserved.
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