Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin.

Protein adsorption on surfaces is a fundamental step in many applications. While various methods such as lithography, self assembly using nanoparticles, layer-by-layer attachment, etc. have been employed, here we report fabrication of controlled nanostructure of a new resilin-mimetic elastic protein rec1-resilin using physical approaches. We investigate the assembly, morphology and tunability of the nanostructure of adsorbed rec1-resilin architectures by atomic force microscopy (AFM) and scanning thermal microscopy (SThm) demonstrating that the protein conformation and structure during assembly can be controlled by tuning the physical conditions at the surface. Our findings show distinct morphology and height of monomolecular rec1-resilin film, dependent on substrate surface energy. We also show that these heights, a function of molecular orientation, can be maintained on swelling and drying.