Peptide-Based Protein Capture Agents with High Affinity, Selectivity, and Stability as Antibody Replacements in Biodetection Assays

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 a...

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Bibliographic Details
Main Authors: Coppock, Matthew B, Farrow, Blake, Warner, Candice, Finch, Amethist S, Lai, Bert, Sarkes, Deborah A, Heath, James R, Stratis-Cullum, Dimitra
Format: Report
Language:English
Subjects:
ANTIBODY REPLACEMENTS
ANTIGENS
BIOASSAY
Biochemistry
BIOLOGICAL DETECTION
CHEMICAL STABILITY
LIGANDS
Miscellaneous Detection and Detectors
MONOCLONAL ANTIBODIES
OLIGOPEPTIDES
PCC AGENTS
PCC(PROTEIN CATALYZED CAPTURE)
PEPTIDE-BASED SENSORS
PEPTIDES
Pharmacology
PROTEIN EPITOPES
PROTEINS
THERMAL STABILITY
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Summary: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. The original document contains color images. Published in Proc. of SPIE v9107, 2014. Prepared in collaboration with the Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, the Edgewood Chemical Biological Center, Aberdeen Proving Ground, MD, and Indi Molecular, Culver City, CA.