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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tian, Zhiyong Zang, Fenglei Luo, Wen Zhao, Zhonghua Wang, Yueqiao Xu, Xuejun Wang, Chaojie |
| Description | Author Affiliation: Tian Z ( Institute of Chemical Biology, Henan University, Kaifeng 475004, PR China.); Zang F ( Institute of Chemical Biology, Henan University, Kaifeng 475004, PR China.); Luo W ( The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng 475004, PR China.); Zhao Z ( Institute of Chemical Biology, Henan University, Kaifeng 475004, PR China.); Wang Y ( Institute of Chemical Biology, Henan University, Kaifeng 475004, PR China.); Xu X ( Huaihe Clinical Institute, Henan University, Kaifeng 475004, PR China. Electronic address: 1322078049@qq.com.); Wang C ( The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng 475004, PR China. Electronic address: wcjsxq@henu.edu.cn.) |
| Abstract | The interaction mononaphthalimide spermidine (MINS, 1) and bovine serum albumin (BSA) was studied by UV/vis absorption, fluorescence and circular dichroism spectra (CD) under physiological conditions (pH=7.4). The observed spectral quenching of BSA by compound 1 indicated compound 1 could bind to BSA. Further fluorescent tests revealed that the quenching mechanism of BSA by compound 1 was overall static. Meanwhile, the obtained binding constant and thermodynamic parameters on compound-BSA interaction showed that the type of interaction force of compound 1 and BSA was mainly hydrophobic. The analysis of synchronous, three-dimensional fluorescence and CD showed that compound 1 had weak influence on the conformational changes in BSA. Molecular docking simulation was performed and docking model in silico suggested that the configuration of compound 1 was localized in enzymatic drug site II in BSA. Furthermore, naphthalimide moiety of compound 1 greatly contributed to the hydrophobic interaction between compound 1 and BSA protein, as confirmed by experimental data. |
| File Format | HTM / HTML |
| ISSN | 10111344 |
| Volume Number | 142 |
| e-ISSN | 18732682 |
| Journal | Journal of Photochemistry and Photobiology B: Biology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-01-01 |
| Publisher Place | Switzerland |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biology Serum Albumin, Bovine Metabolism Spermidine Animals Binding Sites Cattle Circular Dichroism Hydrophobic And Hydrophilic Interactions Molecular Docking Simulation Protein Binding Protein Structure, Tertiary Chemistry Spectrophotometry, Ultraviolet Temperature Thermodynamics Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Radiology, Nuclear Medicine and Imaging Biophysics Radiological and Ultrasound Technology Radiation |
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