Self-Assembling 2D Nano-Crystalline of Recombinant Surface Layer Proteins (S-Layer) on Solid Substrates and Electrical Responses

Abstract

ABSTRACTS-layer proteins of various lattice-forming types are the most abundant protein by mass on earth. They form the outermost cell crystalline component in a broad range of bacteria and archaea. They are porous monomolecular layer with unit cell size in tens of nanometers. These monomer proteins are capable of forming self-assembled mono- or double layers. Isolated from cell surfaces or through recombinant protein production, they are able to form ordered 2D crystal lattice on a variety of non-cellular surfaces. We study S-layer SbpA protein, which is found in mesophilic organism Lysinibacillus sphaericus with square lattice crystallinity. The recombinant SbpA (rSbpA) can be genetically modified and expressed in E. coli in different truncated forms. Using both the wtSpbA and truncated rSbpA, we reproduced the unique two-dimensional self-assembly pattern on several solid or flexible surfaces of interests towards electronic devices. By surface modification we can promote the self-assembly of SbpA on low affinity substrates. This enables a potential mean of creating complex functional bio-nanostructure. Delicate control of the self-assembly processes of S-layer on surfaces also serves the prerequisite of building the supramolecular structure as bio-electronic platform through protein fusing. Understanding of the electrical response from s-layer proteins provides a bridge between biological systems and electronic devices. Scale-up production and understanding the detailed interaction of the S-layer interface will likely be useful for nanobiotechnology and synthetic biology.