Probing the protein conformation and adsorption behaviors in nanographene oxide-protein complexes.
Probing the protein conformation and adsorption behaviors in nanographene oxide-protein complexes.
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DOI：
10.1166/jnn.2014.8521
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发表时间：
2014-03
影响因子：
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通讯作者：
Chunhui Wu;Qiu-hua He;Anni Zhu;Hong Yang;Yiyao Liu
中科院分区：
文献类型：
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作者：
Chunhui Wu;Qiu-hua He;Anni Zhu;Hong Yang;Yiyao Liu
本报告描述了模型蛋白牛血清白蛋白（BSA）吸附在纳米氧化石墨烯（NGO）上的吸附特性和构象变化。在pH 4.0、4.7、7.4和8.8处获得的吸附等温线表明，在pH 4.0的酸性环境中，NGO对BSA的亲和力最高，但蛋白质吸附能力随着pH值的增加而降低。数据表明，BSA 与 NGO 表面的自发结合主要是由于蛋白质构象和静电吸引机制。荧光和同步荧光光谱研究表明，NGO对BSA的荧光有静态和动态猝灭作用，并对BSA的构象以及Trp和Tyr残基周围的微环境产生明显的扰动。此外，通过傅里叶变换红外光谱对蛋白质二级结构的分析表明，吸附后可能会发生明显的二级结构变化。这项研究深入了解了 NGO 和蛋白质之间的相互作用，这对于设计最佳石墨烯纳米片-蛋白质缀合物至关重要。
In this report, the adsorption characteristics and conformation changes of model protein bovine serum albumin (BSA) adsorbed on nanographene oxide (NGO) are described. The adsorption isotherms obtained at pH 4.0, 4.7, 7.4 and 8.8 show that NGO has the highest affinity for BSA in the acid environment of pH 4.0, but the protein adsorption capacity decreases with the pH value increasing. The data imply that the spontaneously binding of BSA to the NGO surfaces is mainly due to the protein conformation and an electrostatic attraction mechanism. The fluorescence and synchronous fluorescence spectroscopic studies show that NGO quenches the fluorescence of BSA both statically and dynamically, and induces obvious perturbations on the conformation of BSA as well as the microenvironments around the Trp and Tyr residues. Moreover, analysis of the secondary structure of the proteins via Fourier transform infrared spectroscopy revealed that evident secondary structural changes may undergo upon adsorption. This study gives an insight into the interaction between NGO and proteins, which is critical in the design of optimal graphene nanosheets-protein conjugates.