Gold nanoparticle capture within protein crystal scaffolds
Gold nanoparticle capture within protein crystal scaffolds
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DOI：
10.1039/c6nr03096c
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发表时间：
2016-01-01
期刊：
影响因子：
6.7
通讯作者：
Snow, Christopher D.
中科院分区：
文献类型：
--
作者：
Kowalski, Ann E.;Huber, Thaddaus R.;Snow, Christopher D.
DNA组装已被用于将无机纳米颗粒组织成3D阵列，由于纳米颗粒的间距和几何形状而产生涌现特性。我们在这里报告使用工程蛋白质晶体作为生物介导的无机纳米粒子组装的替代方法。蛋白质晶体的13 nm直径的孔导致80%的溶剂含量，并在其内部显示六聚组氨酸序列。六组氨酸序列通过Ni（II）与簇和蛋白质的配位在整个化学交联晶体中捕获Au-25（谷胱甘肽）（类似于17）（次氮基三乙酸）（类似于1）纳米簇。通过共聚焦显微镜和元素分析验证纳米颗粒负载。纳米颗粒可以通过暴露于EDTA从晶体中释放，EDTA螯合Ni（II）并破坏特定的蛋白质/纳米颗粒相互作用。通过单晶X射线晶体学证实了交联和纳米颗粒捕获后蛋白质晶体的完整性。
DNA assemblies have been used to organize inorganic nanoparticles into 3D arrays, with emergent properties arising as a result of nanoparticle spacing and geometry. We report here the use of engineered protein crystals as an alternative approach to biologically mediated assembly of inorganic nanoparticles. The protein crystal's 13 nm diameter pores result in an 80% solvent content and display hexahistidine sequences on their interior. The hexahistidine sequence captures Au-25(glutathione)(similar to 17) (nitrilotriacetic acid)(similar to 1) nanoclusters throughout a chemically crosslinked crystal via the coordination of Ni(II) to both the cluster and the protein. Nanoparticle loading was validated by confocal microscopy and elemental analysis. The nanoparticles may be released from the crystal by exposure to EDTA, which chelates the Ni(II) and breaks the specific protein/nanoparticle interaction. The integrity of the protein crystals after crosslinking and nanoparticle capture was confirmed by single crystal X-ray crystallography.