Identification of Clausine E as an inhibitor of fat mass and obesity‐associated protein (FTO) demethylase activity. Issue 10 (19th July 2019)

• Record Type: Journal Article
• Authors: Wang, Ying; Li, Junya; Han, Xinxin; Wang, Ning; Song, Chuanjun; Wang, Ruiyong; Chang, Junbiao
• Is Part Of: Journal of molecular recognition. Volume 32:Issue 10(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-07-19
• Subjects: Clausine E -- fat mass and obesity‐associated protein -- fluorescence -- inhibitor -- isothermal titration calorimetry; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2800
• Languages: English
• ISSNs: 0952-3499

Abstract

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. Abstract : The characteristics of the binding between Clausine E and the fat mass and obesity‐associated protein were investigated by physicochemical and spectroscopic techniques.