Event
Bioengineering Seminar Series: Philip Bryan
Friday, November 1, 2013
9:00 a.m.-10:00 a.m.
Pepco Room, Jeong H. Kim Engineering Building
Yu Chen
yuchen@umd.edu
A 20-Year Perspective on Engineering Proteases: From Damaging Perfectly Good Enzymes to Enzymatic Machines for Biological Computing
Philip Bryan
Professor
Fischell Department of Bioengineering
Institute for Bioscience and Biotechnology Research
University of Maryland
A protease is an enzyme which can control other proteins. Proteases in nature regulate cellular processes from embryogenesis to cell death by linking diverse enzymatic functions together with complex logic gates. We will describe the engineering of the serine protease subtilisin and its prodomain inhibitor to create sophisticated enzymatic machines. Three basic aspects of protease function were modified: activation, specificity, and inhibition. In these enzymatic machines, the protease occupies a role analogous to a transistor in an electronic circuit and is able to mediate such functions as detection, purification, activation, or inactivation (destruction) of other proteins. The substrate protein and the triggering molecule vary from application to application. For example, we have developed a protein purification system (the Profinity eXact Purification System, Bio-Rad). This method uses a simple protease machine for protein purification and provides the conceptual foundation for other devices based on tightly-regulated proteases.
About the Speaker
Pilip Bryan obtained a Ph. D. with Donald Olins at the Biology Division of Oak Ridge National Laboratory where he used biochemical and biophysical approaches to characterize nucleosome structure. His postdoctoral work with Max Birnstiel at the University of Zurich and William Folk at the University of Michigan investigated the role of chromatin structure on the expression of developmentally regulated genes. From 1989 to the present he has applied genetic, biochemical and biophysical methods to the study of protein folding and enzymology at the University of Maryland where he is a professor in the Institute for Bioscience and Biotechnology Research and the Department of Bioengineering. He founded Potomac Affinity Proteins, LLC in 2004 to translate fundamental principles of protein folding and enzymology into protein-based devices for protein purification, ultra-sensitive detection and therapeutics.
