Medalsy Izhar, Dgany Or, Sowwan Mukhles, Cohen Hezy, Yukashevska Alevtyna, Wolf Sharon G, Wolf Amnon, Koster Abraham, Almog Orna, Marton Ira, Pouny Yehonathan, Altman Arie, Shoseyov Oded, Porath Danny
Physical Chemistry Department and Center for Nanoscience and Nanotechnology, The Hebrew University, Jerusalem 91904, Israel.
Nano Lett. 2008 Feb;8(2):473-7. doi: 10.1021/nl072455t. Epub 2008 Jan 15.
Controlled formation of complex nanostructures is one of the main goals of nanoscience and nanotechnology. Stable Protein 1 (SP1) is a boiling-stable ring protein complex, 11 nm in diameter, which self-assembles from 12 identical monomers. SP1 can be utilized to form large ordered arrays; it can be easily modified by genetic engineering to produce various mutants; it is also capable of binding gold nanoparticles (GNPs) and thus forming protein-GNP chains made of alternating SP1s and GNPs. We report the formation and the protocols leading to the formation of those nanostructures and their characterization by transmission electron microscopy, atomic force microscopy, and electrostatic force microscopy. Further control over the GNP interdistances within the protein-GNP chains may lead to the formation of nanowires and structures that may be useful for nanoelectronics.
复杂纳米结构的可控形成是纳米科学和纳米技术的主要目标之一。稳定蛋白1(SP1)是一种直径为11纳米的热稳定环状蛋白复合物,由12个相同的单体自组装而成。SP1可用于形成大型有序阵列;它可以通过基因工程轻松修饰以产生各种突变体;它还能够结合金纳米颗粒(GNP),从而形成由交替的SP1和GNP组成的蛋白质-GNP链。我们报告了这些纳米结构的形成、形成这些纳米结构的实验方案以及通过透射电子显微镜、原子力显微镜和静电力显微镜对其进行的表征。对蛋白质-GNP链内GNP间距的进一步控制可能会导致形成纳米线和对纳米电子学有用的结构。