Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods
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Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods
Chinese Journal of LuminescenceVol. 31, Issue 2, Pages: 285-290(2010)
作者机构:
河北大学理化分析中心 药物化学与分子诊断教育部重点实验室,河北 保定,071002
作者简介:
基金信息:
DOI:
CLC:O657.3;O482.31
Received:25 November 2009,
Revised:02 January 1900,
Published Online:30 April 2010,
Published:30 April 2010
稿件说明:
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LIU Bao-sheng, XUE Chun-li, WANG Jing, et al. Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods[J]. Chinese journal of luminescence, 2010, 31(2): 285-290.
DOI:
LIU Bao-sheng, XUE Chun-li, WANG Jing, et al. Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods[J]. Chinese journal of luminescence, 2010, 31(2): 285-290.DOI:
Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods
both ciprofloxacin (CPFX) and ofloxacin (OFLX) can quench fluorescence of bovine serum albumin (BSA). The fluorescence intensity is obviously gone down when the two drugs coexist. According to this
studies were established on the interaction between CPFX and OFLX by fluorescence spectrum. It was proved that the interaction between the drugs reduces the binding stability of the drug and protein. At the same time
increase of the free drug concentration will increase the effect of the drugs. The result showed that the quenching mechanism of the combination of bovine serum albumin and drugs is a static procedure. The number of binding sites is 1 in several of system. Based on the theory of Frester spectroscopy energy transfer
the binding distance (
r
<7.0 nm) between the drugs and BSA was obtained. It belongs to non-radiation energy transfer. Because of the existence of interaction between the drugs
the correlation coefficient and binding distance are increased. Studies by synchronous spectra show the effect of the interaction between the drugs on conformation of BSA. It makes protein molecules extend and hydrophobic nature reduces.
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references
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