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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jiang, Bingfei Liao, Zhixi Li, Xiaofang Yu, Xianyong |
| Description | Author Affiliation: Yu X ( Key Laboratory of Theoretical Organic Chemistry and Function Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China); Jiang B ( Key Laboratory of Theoretical Organic Chemistry and Function Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China.); Liao Z ( Key Laboratory of Theoretical Organic Chemistry and Function Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China.); Li X ( Key Laboratory of Theoretical Organic Chemistry and Function Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China. Electronic address: lixiaofang@iccas.ac.) |
| Abstract | The interaction between 21-(Ph-NN)-NCTPP and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy under imitated physiological conditions. The results showed that the intrinsic fluorescence of BSA was quenched strongly by 21-(Ph-NN)-NCTPP. The binding constants (Ka) and the binding sites (n) were obtained at three different temperatures (298, 304, and 310K). The thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated, the results indicated that the binding process was spontaneous and the hydrophobic interaction played a major role in [21-(Ph-NN)-NCTPP]-BSA binding process. Based on the Förster non-radiation energy transfer theory, the binding distance from 21-(Ph-NN)-NCTPP to BSA was estimated to be about 3.51nm. What's more, the synchronous fluorescence spectra indicated that the conformation of BSA has not been changed. |
| ISSN | 13861425 |
| Volume Number | 142 |
| e-ISSN | 18733557 |
| Journal | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-05-05 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Porphyrins Metabolism Serum Albumin, Bovine Animals Binding Sites Cattle Energy Transfer Hydrophobic And Hydrophilic Interactions Protein Binding Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Thermodynamics Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation |
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