| 光谱学与光谱分析 |
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| Study on the Interaction of Lomefloxacin Terbium Complex and Bovine Serum Albumin by Fluorescence Spectra |
| HE Hua1,YE Hai-ying1,DAI Li1,JIAO Qing-cai2,CHUONG Pham-Huy3 |
1. China Pharmaceutical University，Nanjing 210009, China
2. Pharmaceutic Biotechnology Key Laboratory，College of Life Science，Nanjing University，Nanjing 210093，China
3. Faculty of Pharmacy, University of Paris V, 4 avenue de l’Observatoire, 75006 Paris, France |
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Abstract Using lomefloxacin-terbium as a fluorescent probe, the interaction of LFLX-Tb3+ and bovine serum albumin (BSA) was investigated by fluorescence spectra. The interaction of LFLX and BSA is quite strong. LFLX can affect the conformation of BSA to some degree. Meanwhile, the electrostatic binding of the BSA with Tb3+ in LFLX-Tb3+ complex could decease the nonradiative energy loss through O—H vibration of H2O molecule in Tb3+ complex. Under the optimum conditions, BSA can enhance the fluorescence intensity of the lomefloxacin-terbium complex at 545 nm, and the enhanced fluorescence intensity of Tb3+ is proportional to the concentration of BSA. Based on that, a new method is constructed for the determination of BSA. The linear ranges for BSA are 16.5-148.5 μg·mL-1 with a detection limit of 68.8 ng·mL-1 and relative standard deviations of 1.4%. This method is simple, practical and relatively free of interference from coexistent substances.
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Received: 2005-01-10
Accepted: 2005-04-28
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Corresponding Authors:
HE Hua
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| Cite this article: |
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HE Hua,YE Hai-ying,DAI Li, et al. Study on the Interaction of Lomefloxacin Terbium Complex and Bovine Serum Albumin by Fluorescence Spectra [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(03): 480-483.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I03/480 |
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