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Electrochemical behaviors of lomefloxacin at a single-wall carbon nanotube-modified electrode and its interaction with bovine serum albumin
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作者 xu maotian KONG Fenying ZHANG Yintang 《商丘师范学院学报》 CAS 2009年第12期46-53,共8页
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
关键词 电化学分析法 电气化学 SCE LMF
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Studies on the Interaction Between Vanillin and β-Amyloid Protein via Fluorescence Spectroscopy and Atomic Force Microscopy
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作者 SONG Shengmei MA xuewen +3 位作者 ZHOU Yehong xu maotian SHUANG Shaomin DONG Chuan 《Chemical Research in Chinese Universities》 SCIE CAS CSCD 2016年第2期172-177,共6页
β-Amyloid(Afl) plaques and intracellular neurofibrillary lesions in the brain are markers of Alzheimer's disease(AD). The ability to safely decrease Aft concentrations is potentially important as a preventive st... β-Amyloid(Afl) plaques and intracellular neurofibrillary lesions in the brain are markers of Alzheimer's disease(AD). The ability to safely decrease Aft concentrations is potentially important as a preventive strategy for AD. The interactions between vanillin and Aft polypeptide were investigated via fluorescence spectroscopy and atomic force microscopy(AFM). The results of fluorescence and synchronous spectroscopies illustrate that the intrinsic fluorescence of tyrosine(Tyr) residues in Aβ1-42 aggregates can be quenched strongly upon the formation of vanil- lin-Aβ-42 complex. Thioflavine T(ThT)-induced fluorescence changes indicated that Aβ1--42 aggregates could be disaggregated by vanillin, and the AFM images of Aβ1-42 enunciated the depolymerization of Aβ1-42 aggregates by vanillin in a dose-dependent manner. Vanillin may be a potential pharmacological agent for the treatment of AD. 展开更多
关键词 β-Amyloid fibril VANILLIN INTERACTION Fluorescence spectroscopy Atomic force microscopy
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