| 光谱学与光谱分析 |
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| Study of the Interaction between Methotrexate and Bovine Serum Albumin by Spectrometry |
| XIE Wen-jun1, FENG Yu-ping1*, CAO Sheng-li2, ZHAO Yu-fen1 |
1. Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology(Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
2. Department of Chemistry, Capital Normal University, Beijing 100037, China |
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Abstract The interaction of methotrexate (MTX) and bovine serum albumin (BSA) was studied by fluorescence and absorption spectra. The results show that methotrexate strongly quenched the fluorescence of bovine serum albumin, and the quenching mechanism is a static quenching procedure. The binding constants and the number of binding sites between MTX and BSA at different temperatures were calculated. Furthermore, the enthalpy and entropy changes in the interaction were also obtained, and the primary binding pattern between MTX and BSA was interpreted as hydrophobic interaction.
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Received: 2005-06-28
Accepted: 2005-11-08
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Corresponding Authors:
FENG Yu-ping
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| Cite this article: |
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XIE Wen-jun,FENG Yu-ping,CAO Sheng-li, et al. Study of the Interaction between Methotrexate and Bovine Serum Albumin by Spectrometry [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(10): 1876-1879.
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https://www.gpxygpfx.com/EN/Y2006/V26/I10/1876 |
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