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Proceedings Paper

Isolation and characterization of anti-SEB peptides using magnetic sorting and bacterial peptide display library technology
Author(s): Joseph M. Pennington; Joshua M. Kogot; Deborah A. Sarkes; Paul M. Pellegrino; Dimitra N. Stratis-Cullum
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Paper Abstract

Peptide display libraries offer an alternative method to existing antibody development methods enabling rapid isolation of highly stable reagents for detection of new and emerging biological threats. Bacterial display libraries are used to isolate new peptide reagents within 1 week, which is simpler and timelier than using competing display library technology based on phage or yeast. Using magnetic sorting methods, we have isolated peptide reagents with high affinity and specificity to staphylococcal enterotoxin B (SEB), a suspected food pathogen. Flow cytometry methods were used for on-cell characterization and the binding affinity (Kd) of this new peptide reagent was determined to be 56 nm with minimal cross-reactivity to other proteins. These results demonstrated that magnetic sorting for new reagents using bacterial display libraries is a rapid and effective method and has the potential for current and new and emerging food pathogen targets.

Paper Details

Date Published: 4 May 2012
PDF: 6 pages
Proc. SPIE 8358, Chemical, Biological, Radiological, Nuclear, and Explosives (CBRNE) Sensing XIII, 83581Z (4 May 2012); doi: 10.1117/12.919778
Show Author Affiliations
Joseph M. Pennington, U.S. Army Research Lab. (United States)
Joshua M. Kogot, U.S. Army Research Lab. (United States)
Deborah A. Sarkes, U.S. Army Research Lab. (United States)
Paul M. Pellegrino, U.S. Army Research Lab. (United States)
Dimitra N. Stratis-Cullum, U.S. Army Research Lab. (United States)


Published in SPIE Proceedings Vol. 8358:
Chemical, Biological, Radiological, Nuclear, and Explosives (CBRNE) Sensing XIII
Augustus Way Fountain, Editor(s)

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