1. Department of Microbiology, Cornell University, Ithaca, NY 14853, USA;2. Department of Food Science, Cornell University, 317 Stocking Hall, Ithaca, NY 14853, USA;3. Alexa Inc., 480 University Avenue, Suite 910 Toronto, Ontario M5G1V2, Canada;4. College of Nanoscale Science and Engineering, University at Albany, Albany, NY 12203, USA;5. Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA
Abstract:
S‐Layer proteins are an example of bionanostructures that can be exploited in nanofabrication. In addition to their ordered structure, the ability to self‐assembly is a key feature that makes them a promising technological tool. Here, in vitro self‐assembly kinetics of SpbA was investigated, and found that it occurs at a rate that is dependent on temperature, its concentration, and the concentration of calcium ions and sodium chloride. The activation enthalpy (120.81 kJ · mol?1) and entropy (129.34 J · mol?1 · K?1) obtained infers that the incorporation of monomers incurs in a net loss of hydrophobic surface. By understanding how the protein monomers drive the self‐assembly at different conditions, the rational optimization of this process was feasible.
