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Identification of Clausine E as an inhibitor of fat mass and obesity‐associated protein (FTO) demethylase activity
Author(s) -
Wang Ying,
Li Junya,
Han Xinxin,
Wang Ning,
Song Chuanjun,
Wang Ruiyong,
Chang Junbiao
Publication year - 2019
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2800
Subject(s) - demethylase , anti obesity , chemistry , enthalpy , carbazole , entropy (arrow of time) , enzyme , small molecule , molecule , biochemistry , obesity , stereochemistry , biology , organic chemistry , endocrinology , thermodynamics , epigenetics , physics , gene
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.