Identification of Clausine E as an inhibitor of fat mass and obesity-associated protein (FTO) demethylase activity

  • J Mol Recognit. 2019 Oct;32(10):e2800. doi: 10.1002/jmr.2800.
Ying Wang  1 ,  Junya Li  1 ,  Xinxin Han  1 ,  Ning Wang  1 ,  Chuanjun Song  1 ,  Ruiyong Wang  1 ,  Junbiao Chang  1  2
Affiliations
  • 1. College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, China.
  • 2. College of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, China.
PMID: 31321808 DOI: 10.1002/jmr.2800
Abstract

The Alkaloids containing a carbazole nucleus are an established class of natural products with wide range of biological activities. A combination of thermodynamic and enzymatic activity studies provides an insight into the recognition of Clausine E by the fat mass and obesity-associated protein (FTO). The binding of Clausine E to FTO was driven by positive entropy and negative enthalpy changes. Results also indicated that the hydroxyl group was crucial for the binding of small molecules with FTO. The structural and thermodynamic information provides the basis for the design of more effective inhibitors for FTO demethylase activity.

Keywords
Clausine E; fat mass and obesity-associated protein; fluorescence; inhibitor; isothermal titration calorimetry.
Products