Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ
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...
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| Format: | Article |
| Language: | English |
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Wiley
2018-01-01
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| Series: | Bioinorganic Chemistry and Applications |
| Online Access: | http://dx.doi.org/10.1155/2018/3063271 |
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| author | Jiaqi Mai Yunlan Li Xiaozhi Qiao Xiaoqing Ji Qingshan Li |
| author_facet | Jiaqi Mai Yunlan Li Xiaozhi Qiao Xiaoqing Ji Qingshan Li |
| author_sort | Jiaqi Mai |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-04b41c35600945d99fc2840b96830675 |
| institution | Kabale University |
| issn | 1565-3633 1687-479X |
| language | English |
| publishDate | 2018-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Bioinorganic Chemistry and Applications |
| spelling | doaj-art-04b41c35600945d99fc2840b968306752025-02-03T01:10:04ZengWileyBioinorganic Chemistry and Applications1565-36331687-479X2018-01-01201810.1155/2018/30632713063271Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγJiaqi Mai0Yunlan Li1Xiaozhi Qiao2Xiaoqing Ji3Qingshan Li4School of Pharmaceutical Science, Shanxi Medical University, Taiyuan 030001, ChinaSchool of Pharmaceutical Science, Shanxi Medical University, Taiyuan 030001, ChinaSchool of Pharmaceutical Science, Shanxi Medical University, Taiyuan 030001, ChinaSchool of Pharmaceutical Science, Shanxi Medical University, Taiyuan 030001, ChinaSchool of Pharmaceutical Science, Shanxi Medical University, Taiyuan 030001, ChinaDiorganotin(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.http://dx.doi.org/10.1155/2018/3063271 |
| spellingShingle | Jiaqi Mai Yunlan Li Xiaozhi Qiao Xiaoqing Ji Qingshan Li Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ Bioinorganic Chemistry and Applications |
| title | Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ |
| title_full | Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ |
| title_fullStr | Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ |
| title_full_unstemmed | Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ |
| title_short | Exploration on the Interaction Ability of Antitumor Compound Bis-[2,6-difluoro-N-(hydroxyl-<κ>O)benzamidato-<κ>O]dibutylitin(IV) with Human Peroxisome Proliferator-Activated Receptor hPPARγ |
| title_sort | exploration on the interaction ability of antitumor compound bis 2 6 difluoro n hydroxyl κ o benzamidato κ o dibutylitin iv with human peroxisome proliferator activated receptor hpparγ |
| url | http://dx.doi.org/10.1155/2018/3063271 |
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