期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 37, 期 17, 页码 4580-4589出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2018.1554511
关键词
Fat mass and obesity-associated protein; isothermal titration calorimetry; molecular modeling
资金
- National Natural Science Foundation of China [81330075]
- Key Science and Technology Plan Project of Henan Province [152102310065]
In this study, the interaction between 3-phenyl-1H-indazole (1a) and the fat mass and obesityassociated (FTO) protein was confirmed by isothermal titration calorimetry (ITC). The structure feature of 1a was different from our previously reported FTO inhibitors (radicicol, N-CDPCB and CHTB); the Cl and diol group in structure motif is critical for inhibitors to bind to FTO. In order to test whether there is specificity for the interaction between FTO and 1a, the interactions between 1a and four important proteins (human serum albumin (HSA), pepsin, catalase and trypsin) were investigated by ITC, spectroscopy and molecular docking methods. ITC results showed spontaneous exothermic reactions occurring between 1a and the proteins except trypsin under investigated conditions. The order of the binding affinity of 3-phenyl-1H-indazole is catalase> HSA> FTO> pepsin. Comparison between ITC and spectral results was made. This work will provide the basis for the design of novel inhibitors for FTO.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据