Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancy peak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction between bovine serum albumin (BSA) and lome...Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancy peak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction between bovine serum albumin (BSA) and lomefloxacin, the experimental condition was established after a large number of tests. Based on the site-binding model, the binding parameters were measured according to the site model by Scatchard.展开更多
The electrochemical behaviors of lomefloxacin at a single-wall carbon nanotube-modified glassy carbon electrode have been investigated by cyclic voltammetry.In a Britton-Robinson buffer (pH 4.5),lomefloxacin yields a ...The electrochemical behaviors of lomefloxacin at a single-wall carbon nanotube-modified glassy carbon electrode have been investigated by cyclic voltammetry.In a Britton-Robinson buffer (pH 4.5),lomefloxacin yields a sensitive and well-defined oxidation peak at ca.1.24 V (vs.SCE) on the modified electrode.Compared with the bare glassy carbon electrode,the oxidation peak current of lomefloxacin significantly increases and the oxidation peak potential positively shifts.Under the optimal conditions,the interaction of lomefloxacin with bovine serum albumin is also investigated.The results indicate that an electrochemically inactive supramolecular complex is formed and the formation of complex between lomefloxacin and bovine serum albumin is an intercalation mechanism.The proposed methods offer a reference for the studies on the biological effects and action mechanism of lomefloxacin with albumins in vivo.展开更多
The interaction of lomefloxacin （LMF） with human serum albumin （HSA） in the presence of copper ions in a physiological medium and its thermodynamic characteristics were investigated by multi-spectroscopy. The expe...The interaction of lomefloxacin （LMF） with human serum albumin （HSA） in the presence of copper ions in a physiological medium and its thermodynamic characteristics were investigated by multi-spectroscopy. The experimental results showed that both LMF and LMF-Cu^2＋ could quench the fluorescence of HSA with a static quenching mechanism, indicating that LMF or LMF-Cu^2＋ could react with HSA. The apparent binding constants/numbers of binding sites were estimated as 4.924± 105 Lomol 1/1.473 for LMF-HSA, 8.990± 104 L·mol^-1/1.785 for LMF- Cu^2＋-HSA, 1.10± 105 L·mol^-1/1.21 for LMF-Cu^2＋ and 7.30± 102 L·mol^-1/0.82 for HSA-Cu^2＋, respectively. AH and AS for LMF-HSA system were calculated to be --2.189 kJ·mol^-1 and 61.25 J·mol^-1·K^-1, while those for LMF-Cu^2＋-HSA system were -7.401 kJ·mol^-1 and 47.63 J·mol^-1·K^-1 Although the values of AH and AS in these two systems were different, the treads were similar, which indicated that electrostatic interactions in these two systems played a major role. According to Forster theory, the distances were given as 5.006 nm for HSA-LMF and 4.709 nm for HSA-LMF-Cu^2＋. Synchronous fluorescence and circular dichroism spectra confirmed further that the conformations of human serum albumin before and after interacting with LMF or LMF-Cu^2＋ were different. All the results revealed that copper ions promoted the interaction of lomefloxacin with human serum albumin.展开更多
文摘Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancy peak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction between bovine serum albumin (BSA) and lomefloxacin, the experimental condition was established after a large number of tests. Based on the site-binding model, the binding parameters were measured according to the site model by Scatchard.
基金National Natural Science Foundation of China (No. 20775047)the Natural Science Foundation of Henan Province (No. 0511022300)
文摘The electrochemical behaviors of lomefloxacin at a single-wall carbon nanotube-modified glassy carbon electrode have been investigated by cyclic voltammetry.In a Britton-Robinson buffer (pH 4.5),lomefloxacin yields a sensitive and well-defined oxidation peak at ca.1.24 V (vs.SCE) on the modified electrode.Compared with the bare glassy carbon electrode,the oxidation peak current of lomefloxacin significantly increases and the oxidation peak potential positively shifts.Under the optimal conditions,the interaction of lomefloxacin with bovine serum albumin is also investigated.The results indicate that an electrochemically inactive supramolecular complex is formed and the formation of complex between lomefloxacin and bovine serum albumin is an intercalation mechanism.The proposed methods offer a reference for the studies on the biological effects and action mechanism of lomefloxacin with albumins in vivo.
基金Project supported by the Science Foundation 0f the National Education Ministry （No. 206096）, the Education Department of Hubei Province （No. Z200522002） and the 0pen Foundation of Hubei Key Laboratory of Biotechnology in Traditional Chinese Medicine （No. 20040201）.
文摘The interaction of lomefloxacin （LMF） with human serum albumin （HSA） in the presence of copper ions in a physiological medium and its thermodynamic characteristics were investigated by multi-spectroscopy. The experimental results showed that both LMF and LMF-Cu^2＋ could quench the fluorescence of HSA with a static quenching mechanism, indicating that LMF or LMF-Cu^2＋ could react with HSA. The apparent binding constants/numbers of binding sites were estimated as 4.924± 105 Lomol 1/1.473 for LMF-HSA, 8.990± 104 L·mol^-1/1.785 for LMF- Cu^2＋-HSA, 1.10± 105 L·mol^-1/1.21 for LMF-Cu^2＋ and 7.30± 102 L·mol^-1/0.82 for HSA-Cu^2＋, respectively. AH and AS for LMF-HSA system were calculated to be --2.189 kJ·mol^-1 and 61.25 J·mol^-1·K^-1, while those for LMF-Cu^2＋-HSA system were -7.401 kJ·mol^-1 and 47.63 J·mol^-1·K^-1 Although the values of AH and AS in these two systems were different, the treads were similar, which indicated that electrostatic interactions in these two systems played a major role. According to Forster theory, the distances were given as 5.006 nm for HSA-LMF and 4.709 nm for HSA-LMF-Cu^2＋. Synchronous fluorescence and circular dichroism spectra confirmed further that the conformations of human serum albumin before and after interacting with LMF or LMF-Cu^2＋ were different. All the results revealed that copper ions promoted the interaction of lomefloxacin with human serum albumin.
