Proteins often deform, dehydrate or otherwise denature when adsorbed or patterned directly onto an inorganic substrate, thus losing specificity and biofunctionality. One method used to maintain function is to pattern the protein of interest directly onto another underlying protein or polypeptide that acts as a buffer layer between the substrate and the desired protein. We have used microcontact printing (μcp) to cross-stamp orthogonal linear arrays of two different proteins (e.g., IgG, poly-lysine, protein A) onto glass substrates. This created three separate types of protein-substrate microenvironments, including crossover structures of protein one on protein two. We report preliminary fluorescent microscopy and scanning force microscopy characterization of these structures, including commonly encountered structural defects.