Diorganotin(IV) antitumor compound bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O] (DBDF2,6T) was one of the novel patent organotin compounds with high antitumor activity and relatively low toxicity. In this study, several methods were used to study the interaction between DBDF2,6T and hPPARγ protein, including fluorescence quenching, three-dimensional (3D) fluorescence, drug affinity responsive target stability (DARTS), ultrafiltration-LC, and molecular docking. According to the experimental results, the quenching process of the hPPARγ protein was induced by static quenching mode to form a nonradiative ground-state complex with DBDF2,6T spontaneously, mainly through the hydrophobic force. DBDF2,6T could bind to the hPPARγ protein directly and give the protein the ability of antienzymatic hydrolysis. And the binding mode of DBDF2,6T into hPPARγ protein appeared to have an orientation towards residues of SER342 and GLY284. In conclusion, these methods could comprehensively reveal the interaction details of DBDF2,6T and the hPPARγ protein and established a feasible way to preliminarily identify the agonist compounds for the hPPARγ protein.

中文翻译：

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抗肿瘤化合物Bis- [2,6-二氟-N-（羟基-<κ> O）苯甲酰胺基-<κ> O]二丁基itin（IV）与人过氧化物酶体增殖物激活受体hPPARγ的相互作用能力的探讨。

二有机锡（IV）抗肿瘤化合物双-[2,6-二氟-N-（羟基-<κ> O）苯甲酰氨基- <κ> O ]（DBDF2,6T）是新型的有机锡专利化合物，具有很高的抗肿瘤活性，并且毒性相对较低。在这项研究中，使用了若干方法来研究和DBDF2,6T hPPAR之间的相互作用γ蛋白质，包括荧光猝灭，三维（3D）荧光，药物亲和力应答靶稳定性（DARTS），超滤-LC，和分子对接。根据实验结果，在hPPAR的淬火工艺γ蛋白质通过静态猝灭模式诱导，主要通过疏水力自发形成与DBDF2,6T的非辐射基态复合物。DBDF2,6T可以绑定到hPPAR γ蛋白质直接给予蛋白水解antienzymatic的能力。和DBDF2,6T到hPPAR的结合模式γ蛋白质似乎有朝着SER342和GLY284的残基的方向。总之，这些方法可以全面揭示DBDF2,6T的交互细节和hPPAR γ蛋白质和建立一个可行的办法，初步确定为hPPAR激动剂化合物γ蛋白质。