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Published May 22, 2014 | Published
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Peptide-based protein capture agents with high affinity, selectivity, and stability as antibody replacements in biodetection assays

Abstract

Current biodetection assays that employ monoclonal antibodies as primary capture agents exhibit limited fieldability, shelf life, and performance due to batch-to-batch production variability and restricted thermal stability. In order to improve upon the detection of biological threats in fieldable assays and systems for the Army, we are investigating protein catalyzed capture (PCC) agents as drop-in replacements for the existing antibody technology through iterative in situ click chemistry. The PCC agent oligopeptides are developed against known protein epitopes and can be mass produced using robotic methods. In this work, a PCC agent under development will be discussed. The performance, including affinity, selectivity, and stability of the capture agent technology, is analyzed by immunoprecipitation, western blotting, and ELISA experiments. The oligopeptide demonstrates superb selectivity coupled with high affinity through multi-ligand design, and improved thermal, chemical, and biochemical stability due to non-natural amino acid PCC agent design

Additional Information

© 2014 Society of Photo-Optical Instrumentation Engineers (SPIE). This research was funded primarily provided by the Institute for Collaborative Biotechnologies through grant W911NF-09-0001 from the U.S. Army Research Office. Research is supported in part by appointments (M.B.C.) to the U.S. Army Research Laboratory Postdoctoral Fellowship Program administered by the Oak Ridge Associated Universities through a contract with the U.S. Army Research Laboratory. The content of the information does not necessarily reflect the position or the policy of the Government, and no official endorsement should be inferred. The following reagents were obtained through the NIH Biodefense and Emerging Infections Research Resources Repository, NIAID, NIH: Anthrax Protective Antigen (PA), recombinant from E. coli, NR-3780.

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