Phage Antibody Selection with Reichert SPR Systems
Dr. Mark Sullivan
Research Assistant Professor, Department of Microbiology and Immunology and Director, Biomolecular Interaction Laboratory, at the University of RochesterDownload a PDF of webinar
The use of surface plasmon resonance to characterize protein:protein interactions is well established and has been the method of choice for determination of antibody affinity for the last 20 years. Developments such as phage display have led to rapid production of numerous antibodies in a high-throughput environment that typically requires affinity analysis to select the proper candidates for further development. Moreover, since most display libraries are limited in terms of the number of sequences in the libraries (typically 1x109 to 1x1010), a frequent result is that initial candidates for development are not of sufficiently high affinity, necessitating affinity improvement strategies. In this presentation, we will describe our studies to demonstrate that the SR7000DC can be used to improve the efficiency of phage antibody isolation and characterization and to evaluate the potential for optimizing selection of high affinity variants. The idea of using an SPR instrument to function as both a lab-on a chip to permit semi-automated manipulation of phage preparations as well as providing the SPR signal as a window on the binding and enrichment of high affinity variants of scFvs or Fabs (or other scaffolds like camelid VHH and fibronectin domains) is appealing, and could lead to a significant competitive advantage in the expanding market for therapeutic antibodies.