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

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.