Eric M Tippmann
New approaches for the optimization of translational and post-translational modification of proteins are presented. We show that nonnatural amino acids (NAAs) are genetically encoded in vivo using a suitable host organism. The amino acids are encoded site-selectively in response to a recoded amber stop codon. The overall goals of our research are to develop novel amino acids, but also to advance the understanding of the mechanism and function of bioorthogonal translation elements. Using the fundamentals of chemistry, NAAs may be chemically tailored to possess specific properties for highly specialised applications, for example, in the charting of biological pathways or in unique post-translational modifications. In these scenarios, there is a synergy between the chemistry of the NAA and the biochemistry of the host organism used to heterologously express the labeled protein. Our recent work has highlighted issues of compatibility between host and NAA (JBC, 2009 284: 28795) as well as increasing the scope for most NAAs (PNAS 2011 doi:10.1073/pnas.1012276108), including photocrosslinkers. By increasing the sophistication of the amber suppression method, a host clear multidisciplinary applications related to drug delivery and biomaterials becomes possible and preliminary work in these directions is presented.
Dr. Tippmann completed his Ph.D at The Ohio State University which was followed by postdoctoral studies at The Scripps Research Institute in La Jolla. He is a research board member of Cardiff Institute of Tissue Engineering and Repair (CITER) and founding member of the Cardiff Physical Organic Chemistry Centre.