Cancer is the second greatest cause of death in the United States. Nevertheless, many biomarkers have been found for various types of cancer, such as pancreatic, breast and prostate cancer. These biomarkers that are intrinsic to a particular form of cancer can be applied to cancer diagnostics and detection, given a specific receptor and reporter. G protein coupled receptors, along with yeast, can be used as a reliable method of cancer detection when enhanced with directed evolution (to induce sensitivity to high concentrations of biomarker, but not low concentrations) and expressed alongside GFP in the presence of a strong signal.

Hemophilia A, the most common type of hemophilia, is caused by a missing or defective factor VIII clotting protein. Current treatments are time-consuming, expensive, and unpleasant. Our idea is to create a probiotic that secretes coagulation factor VIII into the small intestine to be absorbed into the bloodstream. We would obtain cells with mutations in the thioredoxin reductase gene (trxB) and glutathione reductase gene (gor) in order to make E.coli’s intracellular environment oxidizing. This is necessary for the oxidation of the disulfide bonds in the Factor VIII proteins, which along with the expression of a heterologous protein disulfide isomerase and a heterologous chaperone protein, enhances the yield and solubility of Factor VIII proteins. The proteins will be expressed in E.coli, given the appropriate auxotrophic control sequences and gene casette. The production of the factor VIII proteins will be tested via Western Blot, and the activity of the proteins will be observed with a APTT-based one-stage assay. Finally, the solubility of the proteins was evaluated by verifying the presence of the proteins in an aqueous fraction (after centrifugation).

Most collagen products used for biomaterials or biomedical devices are extracted from animal sources. However, application of animal collagen carries the risk of pathogen or prion contamination and the possibility of causing allergies. Other problems include the lack of standardization for animal collagen extraction processes and the inability to modify collagen sequences to achieve different biological purposes. Compared with collagens extracted from animal tissues, recombinant collagens are highly pure, disease free, consistent among batches, and amendable to sequence modifications and large scale production. Such recombinant collagen can be made by E.colibacteria, allowing for the use of versatile and cheap collagen, especially in the fields of regenerative medicine and tissue engineering.