Fabrication of Gold Nanoparticles Inside Unmodified Horse Spleen Apoferritin
Fabrication of Gold Nanoparticles Inside Unmodified Horse Spleen Apoferritin
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DOI：
10.1002/smll.201000457
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发表时间：
2010-07-19
期刊：
影响因子：
13.3
通讯作者：
Orner, Brendan Patrick
中科院分区：
文献类型：
--
作者：
Fan, Rongli;Chew, Shu Wen;Orner, Brendan Patrick
无机纳米材料由于其新兴的特性和在电子、催化、传感器和医疗诊断等众多应用方面的潜力而引起了广泛的关注。[1-3]为了发现未来应用的新特性，人们开发了各种方法来合成无机纳米材料。受自然进化过程的启发，生物系统的使用是其制造的一个新兴趋势，据报道，材料的大小、形状和形态可以通过生物分子和无机材料之间的相互作用来控制蛋白质和多肽由于其巨大的结构和功能多样性以及易于获得，在材料操作中具有很高的实用性。此外，由于所需的温和反应条件，如较低的温度，接近中性的pH值，以及它们通常使用水性反应溶液，生物模板定向合成具有比传统方法更“绿色”的潜力。组装成纳米笼结构的蛋白质经常被用作模板来生产多种类型的纳米颗粒铁蛋白组装成坚固的纳米级笼子，并在原核生物和真核生物中普遍表达。[5-7]例如，来自马脾的铁蛋白由24个亚基组成，形成一个八面体中空球体，外径为12nm，内腔为7nm。铁蛋白的功能是在腔内隔离和矿化铁(O) OH，以防止细胞质和血清铁形成破坏细胞的活性氧。[8,9]铁通过三重对称轴上的8个亲水性通道运输到空腔中，并在蛋白质外壳内矿化。据推测，在脱矿过程中，四重轴上的通道是阳离子的出口通道
Inorganic nanomaterials have attracted extensive attention as a result of their emerging properties and their potential for a multitude of applications such as electronics, catalysis, sensors, and medical diagnosis.[1–3] With the hope of discovering novel properties for future applications, various methods have been developed to synthesize inorganic nanomaterials. The use of biological systems, inspired by naturally evolved processes, is an emerging trend in their fabrication, and it has been reported that material size, shape, and morphology can be controlled by interactions between biomolecules and inorganic materials.[4] Proteins and peptides, due to their large structural and functional diversity and their ready availability, have high utility in the manipulation of materials. Moreover, biotemplate-directed syntheses have the potential to be more ‘‘green’’than traditional methods due to the required mild reaction conditions such as lower temperature, near-neutral pH, and the fact that they often employ aqueous reaction solutions. Proteins that assemble into nanocage structures have often been utilized as templates to produce many types of nanoparticles.[4] The ferritin proteins assemble into robust nanoscale cages and are ubiquitously expressed in both prokaryotes and eukaryotes.[5–7] The ferritin protein from horse spleen, for example, is composed of 24 subunits that form an octahedral, hollow sphere with an exterior diameter of 12nm and an interior cavity of 7 nm. The function of ferritin is to sequester and mineralize Fe (O) OH inside the cavity so as to prevent cytosolic and serum iron from forming cell-destructive, reactive oxygen species.[8, 9] Iron is transported into the cavity through eight hydrophilic channels on the threefold symmetry axes and mineralized within the protein shell. It has been speculated that channels on the fourfold axes serve as exit pathways for cations during demineralization.[10]