光谱学与光谱分析 |
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Interaction of Surface Active Fluorescence Probes and Bovine Serum Albumin |
XU Tong-kuan, LI Na, SHEN Xing-hai*, GAO Hong-cheng |
Department of Applied Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China |
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Abstract The binding between two surface-active substituted 3H-indole fluorescence probes, i.e., iodo-dihexadecyl methyl-2-(p-dodecyl amino phenyl)-3, 3-dimethyl-5-carboethoxy-3H-indole ammonium and iodo-dimethyloctadecyl-2-(p-dodecyl amino phenyl)-3,3-dimethyl-5-carboethoxy-3H-indole ammonium, and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence. The binding constant and binding site number of molecule 1 and molecule 2 with BSA were obtained. It was confirmed that electrostatic interaction is the primary driving force for the combination of BSA with molecule 1 or molecule 2. According to the Frster resonance energy transfer theory, the distances between molecule 1, molecule 2 and tryptophan of BSA were calculated to be 2.90 nm and 4.02 nm, respectively.
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Received: 2004-03-01
Accepted: 2004-06-06
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Corresponding Authors:
SHEN Xing-hai
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Cite this article: |
XU Tong-kuan,LI Na,SHEN Xing-hai, et al. Interaction of Surface Active Fluorescence Probes and Bovine Serum Albumin[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(09): 1443-1445.
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URL: |
https://www.gpxygpfx.com/EN/Y2005/V25/I09/1443 |
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