Antibodies are watchdogs of human health, continuously prowling the body and registering minute changes associated with infection or disease with astonishing acuity. They also serve as biochemical memory banks, faithfully recording information about pathogens they encounter and efficiently storing this data for later use.
Stephen Albert Johnston, Neal Woodbury and their colleagues at the Biodesign Institute at Arizona State University have been exploring mechanisms of antibody activity, particularly the ability of these sentries to bindwith high affinity and specificityto their protein targets. A more thorough understanding of the antibody universe may lead to a new generation of rapid, low-cost diagnostic tools and speed the delivery of new vaccines and therapeutics.
Borrowing a script from nature, the group has been working to construct synthetic antibodies or synbodies, through a simple method developed in Johnston's Center for Innovations in Medicine. They have also examined the broad portrait of antibody activity revealed in a sample of blood, harnessing this information for the presymptomatic diagnosis of disease. These immunosignatures, as Johnston has named them, provide a dynamic report card on human health.
In a pair of new papers, the group demonstrated a simple means of improving the binding affinity of synbodies, which are composed of 20 unit chains of amino acids, strung together in random order. They also used random peptide sequences spotted onto glass microarray slides to mine information concerning the active regions or epitopes of naturally occurring antibodies. These two projects recently appeared in the journals PloS ONE and Molecular and Cellular Proteomics, respectively.
While antibodies have been in use for biomedical research for a long time, conventional techniques for producing them have been time consuming and expensive. Normally, antibodies used for research are produced in animals,
|Contact: Joe Caspermeyer|
Arizona State University