Molecular Bioengineering, Protein Biochemistry and Biotechnology, Cell and Tissue Engineering

Research in the Cochran Laboratory draws upon chemistry, biology, and engineering to create molecular tools for investigating biochemical and biophysical mechanisms. We are using chemical synthesis, directed evolution, and molecular design techniques to develop proteins and materials with specific biological functions. Detailed understanding of the properties of protein-protein interactions and quantitative studies of cell signaling will provide insight into molecular recognition in complex biological systems that can be applied to the development of protein therapeutics. Clinical applications of our research involve bone and wound healing, neural cell regeneration, vascular tissue engineering, and cancer therapy.

Cochran, J. R., Olsen, M. J., Kim, Y., Bhandari, R. B., and Wittrup, K. D. (2004) Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments. J. Immunol. Methods, 287, 147-158.

Johns, T. G., Adams, T. E., Cochran, J. R., Hall, N. E., Hoyne, P. A., Olsen, M. J., Kim, Y. S., Rothacker, J., Nice, E. C., Walker, F., Old, L. J., Ward, C. W., Burgess, A. W., Wittrup, K. D., and Scott, A. M. (2004) Fine epitope mapping of the EGFR-Specific monoclonal antibody 806 reveals that it preferentially recognizes a transitional untethered form of the receptor. J. Biol. Chem, 279, 30375-84.

Feldhaus, M. J., Siegel, R. W., Opresko, L. K., Coleman, J. R., Yeung, Y. A., Cochran, J. R., Heinzelman, P. J., Colby, D., Swers, J., Graff, C., Wiley, H. S., and Wittrup, K. D., (2003) Flow cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nature Biotechnol., 21,163-70.

Cochran, J. R., Aivazian, D. A., Cameron, T. O., and Stern, L. J. (2001) Receptor clustering and transmembrane signaling in T cells. Trends in Biochem. Sci., 26, 304-310.

Cochran, J. R., Cameron, T. O. and Stern, L. J. (2000) The relationship of MHC-peptide binding and T-cell activation probed using chemically-defined MHC class II oligomers. Immunity, 12, 241-250.