Journal
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
Volume 149, Issue -, Pages 290-295Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2017.11.007
Keywords
Fat mass and obesity-associated protein; Analogues; Isothermal titration calorimetry; Fluorescence
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Funding
- National Natural Science Foundation of China [81330075]
- Key science and technology plan project of Henan province [152102310065]
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In this work, the interactions between fat mass and obesity-associated (FTO) protein and three fluoronucleoside analogues (three-member-ring compound (1a), five-member-ring compound (1b) and six-member-ring compound (1c)) have been investigated by fluorescence, ultraviolet-visible absorption spectroscopy, isothermal titration calorimetric (ITC) and molecular modeling. Analysis of fluorescence data showed that the binding between three analogues and FTO occurred via a static quenching mechanism. Both ITC and fluorescence results indicated that 1b is the strongest quencher. In contrast to spectroscopy techniques, ITC results suggested that there is no binding for 1c. ITC results showed that the binding between FTO and 1a (or 1b) were exothermic. Fluorescence results showed that the binding between three analogues and FTO were endothermic. Results of thermodynamic analysis and molecular modeling suggested that it was entropy driven event between FTO and 1a (or 1b). (C) 2017 Elsevier B.V. All rights reserved.
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