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超细ZnFe2O4纳米晶与蛋白质的相互作用

李强 ,  姬晓旭 ,  钟秋 ,  黄新堂 ,  熊丽

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引用本文: 李强, 姬晓旭, 钟秋, 黄新堂, 熊丽. 超细ZnFe2O4纳米晶与蛋白质的相互作用[J]. 无机化学学报, 2013, 29(11): 2375-2381. doi: 10.3969/j.issn.1001-4861.2013.00.368 shu
Citation:  LI Qiang, JI Xiao-Xu, ZHONG Qiu, HUANG Xin-Tang, XIONG Li. Ultrafine ZnFe2O4 Nanocrystals Interacting with Proteins[J]. Chinese Journal of Inorganic Chemistry, 2013, 29(11): 2375-2381. doi: 10.3969/j.issn.1001-4861.2013.00.368 shu

超细ZnFe2O4纳米晶与蛋白质的相互作用

  • 基金项目:

    国家自然科学基金(No.51172085)资助项目。 (No.51172085)

摘要: 水热法制备了超细ZnFe2O4纳米晶,并通过高分辨透射电镜(HRTEM)、XRD和EDX技术对其进行了表征。以牛血清白蛋白(Bovine Serum Albumin,BSA)和牛血红蛋白(Hemoglobin)为模式蛋白,研究了纳米晶在不同pH条件下对蛋白质分子的吸附及其与ζ电势的关系。通过动态光散射(Dynamic Light Scattering,DLS)和傅立叶变换红外光谱(Fourier Transform Infrared,FTIR)技术分别研究了纳米晶吸附蛋白后流体力学直径的变化以及蛋白质构象的变化。结果表明,ZnFe2O4纳米晶对牛血红蛋白的吸附符合静电吸附的规律,而对BSA的吸附则不符合静电吸附的规律。纳米晶吸附牛血红蛋白后主要以单体和三聚体的形式存在,仅存在少量的团聚体,而吸附BSA后完全以团聚体的形式存在。FTIR光谱则显示纳米晶对牛血红蛋白构象的影响大于对BSA构象的影响。在合适的pH条件下,纳米晶对BSA及牛血红蛋白的吸附容量均超过380mg·g-1,有望应用于蛋白质的高效分离。

English

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  • 收稿日期:  2013-05-08
  • 网络出版日期:  2013-06-20
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