The adsorption mechanism and induced conformational changes of three typical proteins with different secondary structural features on graphene
The adsorption mechanism and induced conformational changes of three typical proteins with different secondary structural features on graphene
复制标题
具有不同二级结构特征的三种典型蛋白质在石墨烯上的吸附机理及诱导构象变化
DOI：
10.1039/c3ra45876h
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发表时间：
2014-01-01
期刊：
影响因子：
3.9
通讯作者：
Liu, Huanxiang
中科院分区：
文献类型：
--
作者：
Guo, Jingjing;Yao, Xiaojun;Liu, Huanxiang
纳米材料在生物医学领域有着广泛的应用。为了探索石墨烯作为最广泛使用的纳米材料之一的生物学效应，我们研究了代表不同二级结构的蛋白质在石墨烯上的吸附行为和诱导的构象变化：β-链（WW结构域）、混合α/β结构（BBA蛋白）和α-螺旋（λ-阻遏物）。我们的研究结果表明，这些模型蛋白质吸附在石墨烯表面迅速，紧密，但不同程度的构象变化观察。在吸附过程中，我们发现β模体是一个比α-螺旋更硬的结构单元。此外，蛋白质的构象变化的水平不仅与它们的序列和结构性质有关，而且与它们的取向有关。总体而言，从不同水平的分子间相互作用来看，蛋白质吸附主要由货车范德华力、疏水力和π-π堆积力驱动。我们的工作表明，经典的分子动力学模拟和MM-GBSA计算可以提供有用的信息的动力学和能量的蛋白质吸附到石墨烯上。我们相信这些发现将有助于我们在原子水平上进一步了解蛋白质在疏水碳纳米材料上的吸附。
Nanomaterials (NMs) have been widely used in the biomedical field. To explore the biological effects of graphene as one of the most widely used NMs, we studied the adsorption behavior and induced conformational changes of proteins representing different secondary structures on graphene: β-strands (WW domain), mixed α/β structure (BBA protein), and α-helices (λ-repressor). Our results indicate these model proteins were adsorbed onto the graphene surface quickly and tightly, however, varied degrees of conformational changes were observed. During the adsorption process, we found the β motif is a stiffer structural unit than the α-helix. Moreover, the level of conformational changes of the proteins is related not only to their sequence and structural properties but also to their orientation. Overall, from the different levels of intermolecular interaction, the protein adsorption was driven by van der Waals, hydrophobic and π–π stacking interactions. Our work suggests that classical molecular dynamics simulations and MM-GBSA calculations can provide useful information about the dynamics and energetics of the adsorption of proteins onto graphene. We believe that these findings will help us to further understand the adsorption of proteins on hydrophobic carbon nanomaterials at the atomic level.