Self-assembled Magnetic Nanoparticle Arrays: Rod-like Scaffold Proteins to Precisely Template the Spatial Organisation of Biomineralisation Proteins

随着革命性的纳米技术是如何精确合成的最终野心，Staniland集团正在开发一种整体的自下而上的制造方法，利用生物组件的纳米级精度，自组装和生物矿化来组装数据存储平台。最近，我们开发了使用MNP生物矿化蛋白Mms6.1，2在表面图案中的精确磁铁矿磁性纳米颗粒（MNP）的生物矿化。同样，我们最近在表面上图案化了另一种（MIA）3蛋白，具有高亲和力MNP结合，可用于在特定图案位置定位预形成的MNP。此外，我们发现在表面上研究这个系统可以为Mms蛋白的作用提供关键的见解。然而，我们仍然无法控制每个位置Mms蛋白的确切数量。Potts小组最近鉴定并表征了一种细长的蛋白质支架（SasG）5，其几何形状和刚性非常适合自组装成纳米级网络图案。该系统提供了一个有吸引力的综合路线，其中生物矿化和支架蛋白可以共同修饰和共同表达，以产生自组装生物矿化，最终可能导致精确的数据存储介质。此外，SasG支架可以用Mms和MIA蛋白在预定的位点以明确的间距进行修饰，从而更深入地了解密度在生物矿化蛋白功能中的作用。最后，约翰逊集团提供独特的分析技术，包括QCM-D和FT-IR，使表面固定的生物分子的结构和功能的详细研究。

With the ultimate ambition of revolutionising how precise nanotechnology is synthesized, the Staniland group are developing a holistic bottom-up fabrication methodology exploiting the nanoscale precision of biological components, self-assembly and biomineralisation to assemble data-storage platforms. Recently we developed biomineralisation of precise magnetite magnetic nanoparticles (MNPs) in patterns on surfaces using MNP biomineralisation protein Mms6.1,2 Similarly, we've recently patterned another (MIA)3 protein on the surface with high-affinity MNP binding and can be used to locate pre-formed MNPs at specific patterned locations. Furthermore, we have found that studying this system on a surface can provide crucial insight into the action of the Mms proteins. However, we still cannot control the exact number of Mms proteins at each location. The Potts group have recently identified and characterized an elongated protein scaffold (SasG)5 with a geometry and rigidity that are ideally suited for self-assembly into nanoscale network patterns. The system offers an attractive integrated route where biomineralisation and scaffold proteins can be co-modified and co-expressed, to produce self-assembling biomineralisation that could eventually lead to precise data-storage media. Furthermore the SasG scaffold can be modified with Mms and MIA proteins at pre-determined sites with well-defined spacing, offering greater insight into understanding the role of density in the function of the biomineralisation proteins. Finally, the Johnson group offer unique analytical techniques including QCM-D and FT-IR that enable detailed studies of the structure and function of surface-immobilized biomolecules.