Protein Corona on Gold Nanoparticles Studied with Coarse-Grained Simulations
Protein Corona on Gold Nanoparticles Studied with Coarse-Grained Simulations
复制标题
DOI：
10.1021/acs.langmuir.0c02767
复制
发表时间：
2020-11-10
期刊：
影响因子：
3.9
通讯作者：
Wei, Tao
中科院分区：
文献类型：
--
作者：
Sajib, Md Symon Jahan;Sarker, Pranab;Wei, Tao
在分子和原子水平上理解水性环境中蛋白质冠的形成对于生物分子检测和药物递送等应用至关重要。在这项工作中，我们采用介观粗粒度模拟研究裸金纳米颗粒上的ovipirin-1和溶菌酶蛋白质冠。我们的研究表明，蛋白质冠的形成取决于蛋白质与表面和蛋白质与蛋白质的相互作用以及表面疏水效应。冠状结构被认为是依赖于蛋白质的类型和纳米颗粒的大小。与金NP表面上的溶菌酶的不均匀的多层聚集体相比，Ovispirin蛋白形成均匀的单层吸附。纳米颗粒尺寸的减小导致蛋白质吸附取向的更多角自由度。随后的原子分子动力学模拟进一步证明了在吸附和它的局部结构的异质性的损失的卵螺旋素的二级结构。
Understanding protein corona formation in an aqueous environment at the molecular and atomistic levels is critical to applications such as biomolecule-detection and drug delivery. In this work, we employed mesoscopic coarse-grained simulations to study ovispirin-1 and lysozyme protein coronas on bare gold nanoparticles. Our study showed that protein corona formation is governed by protein-surface and protein-protein interactions, as well as the surface hydrophobic effect. The corona structure was found to be dependent on protein types and the size of nanoparticles. Ovispirin proteins form homogeneous single-layered adsorption in comparison with the lysozyme's inhomogeneous multilayered aggregates on gold NP surfaces. The decrease in nanoparticle size leads to more angular degrees of freedom for protein adsorption orientation. Subsequent atomistic molecular dynamics simulations further demonstrate the loss of secondary structure of ovispirin upon adsorption and the heterogeneity of its local structure.