Hydration Patterns of Graphene-Based Nanomaterials (GBNMs) Play a Major Role in the Stability of a Helical Protein: A Molecular Dynamics Simulation Study
Hydration Patterns of Graphene-Based Nanomaterials (GBNMs) Play a Major Role in the Stability of a Helical Protein: A Molecular Dynamics Simulation Study
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DOI：
10.1021/la4033805
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发表时间：
2013-11-19
期刊：
影响因子：
3.9
通讯作者：
Dhawan, Alok
中科院分区：
文献类型：
--
作者：
Baweja, Lokesh;Balamurugan, Kanagasabai;Dhawan, Alok
石墨烯基纳米材料（GBNM）[氧化石墨烯（GO）、还原氧化石墨烯（rGO）和石墨烯]已被认为是从生物传感平台到蛋白质和肽的细胞递送的各种生物医学应用的潜在候选物。然而，GBNM诱导的蛋白质构象变化是实现其在上述应用中的全部潜力的主要关注点。尽管有几项研究，GBNM对蛋白质构象的影响仍然没有很好的理解。因此，尝试了研究GBNMs对带正电荷的细胞质蛋白质的吸附和构象的影响，使用分子动力学（MD）模拟。我们的研究表明，蛋白质在GO上的吸附是高度选择性的，并通过静电相互作用（氢键/盐桥相互作用）介导，而货车德瓦尔斯和π-π堆积相互作用是蛋白质在rGO和石墨烯上吸附的主要驱动力。二级结构分析表明，蛋白质在GO上的构象稳定性可能归因于GO表面的广泛水化以及与GO的pi区域的pi-pi堆叠中没有酪氨酸残基。GO表面充当类似于存在于生理环境中的蛋白质的天然受体的氢键受体。该计算研究还探索了GO的人工蛋白质受体样潜力。
Graphene-based nanomaterials (GBNMs) [graphene oxide (GO), reduced graphene oxide (rGO), and graphene] have been recognized as potential candidates for various biomedical applications ranging from biosensing platform to cellular delivery of proteins and peptides. However, GBNMs induced conformational changes in proteins are the major concerns in realizing their full potential in aforementioned applications. Despite several studies, the effect of GBNMs on the conformation of proteins is still not well understood. Therefore, an attempt was made to investigate the effect of GBNMs on the adsorption and conformation of positively charged cytoplasmic protein using molecular dynamics (MD) simulations. Our study showed that the adsorption of protein on GO was highly selective and mediated through electrostatic interactions (hydrogen bond/salt bridge interactions), whereas the van der Waals and pi-pi stacking interactions were the major driving forces for the adsorption of protein on rGO and graphene. The secondary structure analysis showed the conformational stability of the protein on GO may be attributed to the extensive hydration of GO surface and the absence of tyrosine residues in pi-pi stacking with pi regions of GO. The GO surface acts as a hydrogen bond acceptor similar to the protein's natural receptor present in a physiological environment. This computational study has also explored the artificial protein receptor like potential of GO.