Protein therapeutics are a front line approach to treatments for cancer, infections, autoimmune disorders, and other diseases. Developing new protein-based therapeutics require methodologies, particularly directed evolution, that enable the engineering of protein-protein interactions with high specificity and affinity. Due to the iterative mutagenesis required for directed evolution, optimizing protein interactions can become tedious. To enhance enrichment of desired variants Team UAlberta designed a protein-protein interaction assay based on the reconstitution of adenylate cyclase in Escherichia coli to accelerate screening for successful variants. We have built two constructs to act as reporters for our system. The first contains genes required for gas vesicle formation and bacterial buoyancy while the second encodes for fluorescent proteins. We will present our results in characterizing the individual components of our project.