Second-degree burns damage the epidermis and part of the dermis, resulting in scar formation during wound healing. During the proliferative phase, activation of TGF-β1 causes fibroblasts to differentiate into myofibroblasts, which rapidly deposit type III collagen, often poorly aligned and contributing to thick scar tissue. In early remodeling, type III collagen is gradually replaced by type I collagen, and fiber organization remains modifiable. Unlike post-scar treatments that cannot influence collagen alignment, our approach targets scar formation while it is actively occurring. We will use Escherichia coli, a non-pathogenic bacterial chassis, to produce RsaA S-layer proteins, which self-assemble into rigid hexagonal lattices and form a temporary, two-dimensional mesh. The proteins are then harvested and applied in an external patch. This mesh delivers nanoscale mechanical cues that provide contact guidance. By mimicking the structural features of the extracellular matrix, the lattice directs cell alignment, ensuring that as type III collagen is replaced by type I, the resulting fibers are organized. Successful protein production will be verified using a GFP reporter, and lattice formation will be confirmed through imaging techniques such as electron microscopy. This project presents a safe, preventative strategy to reduce scar formation following second-degree burns.