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溶菌酶-蛋白质与奈米钻石/奈米硅土之吸附反应动力学

Adsorption Reaction Dynamics of Systems Lysozyme and Nanodiamond/Nanosilica at pH=7-13
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摘要 利用传统荧光光谱法探讨了在pH=7、9、11、13下,各为100nm直径的纳米钻石及纳米硅土(配成0.25μg/μL悬浮液)表面上与用7.0mmol/LPPBS配制成不同浓度溶菌酶-蛋白质之吸附反应.获得了溶菌酶在0-1000mmol/L不同浓度和不MpH值下的吸附反应常数及表面覆盖度.估算得到并讨论不同浓度和不同pH值下附着在纳米颗粒表面上溶菌酶分子的螺旋曲度及构型、每一溶菌酶分子所拥有之表面积大小.两吸附反应系统中,最高的吸附量与最佳的分子构型是在pH=13的环境下.又得到了溶菌酶在约150-250nmol/L的线性覆盖曲区中及4个pH值范围中,可保持最佳活性及构型情况下,每平米纳米钻石及纳米硅土表面积可负载2和10mg,每克纳米钻石及纳米硅土表面可承载溶菌酶130与150mg.在临界浓度下及4个pH值范围中,可配制成最紧密、最大承载的溶菌酶量,每平米纳米钻石及纳米硅土表面积可负载201-55mg,每克纳米钻石及纳米硅土表面可承载810-1680及580-1100mg的溶菌酶. Adsorption reactions between surfaces of nanodiamond and nanosilica with diameter of 100 nm prepared as suspension solutions of 0.25μg/μL and lysozyme molecule with different concentrations of 7 mmol/L PPBS at pH=7, 9, 11, and 13 have been investigated by fluores- cence spectroscopy. Adsorption reaction constants and coverages of lysozyme with different concentrations of 0-1000 nmol/L under the influences of different pH values have been ob- tained. Helicities and conformations of the adsorbed lysozyme molecules, free spaces of every adsorbed lysozyme molecule on the surfaces of nanopartieles at different concentrations and pH values have been deduced and discussed. The highest adsorption capabilities for both sys- tems and conformational efficiency of the adsorbed lysozyme molecule at pH=13 have been obtained. Lysozyme molecules can be prepared, adsorbed and carried with optimal activity and helicity, with 2 and 10 mg/m2 on unit nanosurface, 130 and 150 mg/g with respect to the weight of nanoparticle, within the linear regions of the coverages at around 150-250 nmol/L and four pH values for nanodiamond and nanosilica, respectively. They can be prepared in the tightest packed form, with 20 and 55 mg/m2, 810-1680 and 580-1100 mg/g at threshold concentrations and four pH values for nanodiamond and nanosilica, respectively.
出处 《Chinese Journal of Chemical Physics》 SCIE CAS CSCD 2013年第3期295-302,I0003,I0004,共10页 化学物理学报(英文)
关键词 蛋白质吸附 界面反应动力学 荧光光谱学 单分子光谱学 生物芯片 蛋白质体学 Protein adsorption, Interracial reaction dynamics, Fluorescence spectroscopy,Single molecular spectroscopy, Biochip, Proteomics
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