Assembly of nanoparticle-protein binding complexes: From monomers to ordered arrays
Assembly of nanoparticle-protein binding complexes: From monomers to ordered arrays
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DOI：
10.1002/anie.200701180
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发表时间：
2007-01-01
影响因子：
16.6
通讯作者：
Hainfeld, James F.
中科院分区：
文献类型：
--
作者：
Hu, Minghui;Qian, Luping;Hainfeld, James F.
纳米颗粒（NP）-生物分子结合复合物在成像、传感、催化、电子学和细胞靶向方面显示出有前景的应用，因为纳米颗粒具有尺寸依赖性的光学、电学和磁性特性，而生物分子可以执行独特的生物功能。 [1]以生物分子为模板构建了具有各种结构的NP-生物分子杂化结构。[2]同时，位点特异性识别已广泛应用于许多需要生物分子结构控制的应用中。 [3]尽管生物分子本身显示出多种组装特性，[4] NP 已被用作模板，通过与 DNA、[5] 蛋白质、[6] 和病毒衣壳的相互作用构建 NP-生物分子结合复合物。 [7]然而，功能化纳米粒子作为组装蛋白质模板的潜力尚未得到充分开发，并且纳米粒子-蛋白质纳米结构的控制仍然具有挑战性。在此，我们报告了通过定制结合纳米粒子的大小和蛋白质中遗传标签的位置，形成了具有受控几何形状、化学计量、方向和特异性的纳米粒子-蛋白质杂化复合物。明确的纳米颗粒-蛋白质复合物是通过蛋白质中的 6 个组氨酸 (His) 标签与尺寸范围为 1 至 4 nm 的金纳米颗粒上的次氮基三乙酸镍 (Ni-NTA) 官能团之间的位点特异性结合形成的。我们的研究表明，纳米颗粒不仅是组装功能生物分子的有吸引力的模板，而且还为构建混合纳米颗粒-蛋白质复合物的新颖几何和拓扑结构提供了基础。在这项研究中，我们合成了一个含有配体的NTA部分，(1S)-N-[5-[(4-巯基丁酰基)氨基]-1-羧基戊基]亚氨基二乙酸(NTA-Lys-SH)（参见支持信息中的方案S1）。 [8]该配体用于从 Au (PPh3) 8Cl3 合成 1.3 nm NTA Au NP（参见支持信息中的方案 S2 和图 S1）[9]，并从 HAuCl4 合成 4.4 nm NTA Au NP（参见支持信息中的方案 S3 和图 S2），然后进行反应
Nanoparticle (NP)–biomolecule binding complexes have shown promising applications in imaging, sensing, catalysis, electronics, and cell targeting because NPs possess sizedependent optical, electrical, and magnetic properties while biomolecules can perform unique biological functionalities.[1] NP–biomolecule hybrid structures with various architectures have been constructed by using biomolecules as templates.[2] Meanwhile, the site-specific recognition has been extensively employed for many applications that require biomolecule structural control.[3] Although biomolecules themselves show versatile assembling properties,[4] NPs have been used as templates to construct NP–biomolecule binding complexes through interactions with DNA,[5] proteins,[6] and viral capsids.[7] However, the potential of functionalized NPs as templates to assemble proteins has not been fully explored, and the control of NP–protein nanostructures remains challenging.Herein, we report the formation of NP–protein hybrid complexes with controlled geometry, stoichiometry, orientation, and specificity by tailoring the sizes of binding NPs and placement of genetic tags in proteins. Well-defined NP–protein complexes are formed through site-specific binding between 6 histidine (His) tags in proteins and nickelnitrilotriacetic acid (Ni-NTA) functional groups on Au NPs with sizes ranging from 1 to 4 nm. Our study demonstrates that NPs are not only appealing templates for assembling functional biomolecules, but also provide a mortar to construct novel geometrical and topological architectures of hybrid NP–protein complexes. In this study, we synthesized a ligand-containing NTA moiety,(1S)-N-[5-[(4-Mercaptobutanoyl) amino]-1-carboxypentyl] iminodiacetic acid (NTA-Lys-SH)(see Scheme S1 in the Supporting Information).[8] This ligand was used to synthesize 1.3-nm NTA Au NPs from Au (PPh3) 8Cl3 (see Scheme S2 and Figure S1 in the Supporting Information)[9] and 4.4-nm NTA Au NPs from HAuCl4 (see Scheme S3 and Figure S2 in the Supporting Information) followed by reac-