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

Staniland团队的终极目标是彻底改变精确的纳米技术合成方式，他们正在开发一种整体的自下而上的制造方法，利用生物成分的纳米级精度、自组装和生物矿化来组装数据存储平台。最近，我们利用MNP生物矿化蛋白Mms6.1,2在表面图案上开发了精确的磁铁矿磁性纳米颗粒（MNPs）的生物矿化。同样，我们最近在表面上用高亲和力的MNP结合对另一种（MIA）3蛋白进行了图案化，可用于在特定图案位置定位预形成的MNPs。此外，我们发现在表面上研究这个系统可以为Mms蛋白的作用提供重要的见解。然而，我们仍然无法控制每个位置的Mms蛋白的确切数量。Potts团队最近发现并描述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模式。该系统提供了一种有吸引力的集成途径，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蛋白在预先确定的位置进行修饰，并具有明确的间距，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，Johnson团队提供了独特的分析技术，包括QCM-D和FT-IR，可以详细研究表面固定化生物分子的结构和功能。

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.