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Screening of LPS-specific peptides from a phage display library using epoxy beads

Authors
Kim, YGLee, CSChung, WJKim, EShin, DSRhim, JHLee, YSKim, BGChung, JH
Issue Date
Apr-2005
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
peptide library; lipopolysaccharide; phage display
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.329, no.2-3, pp 312 - 317
Pages
6
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
329
Number
2-3
Start Page
312
End Page
317
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/148790
DOI
10.1016/j.bbrc.2005.01.137
ISSN
0006-291X
1090-2104
Abstract
The selection of identical or highly homologous peptides from phage display combinatorial peptide libraries has been unsuccessful in bioparming experiments using microtiter plates. In the present study, by biopanning on LPS-conjugated epoxy beads, we repeatedly enriched clones encoding AWLPWAK and NLQEFLF. These peptides were found to interact with the polysaccharide moiety of LPS, which is highly variable among gram negative bacterial species. In addition, phages encoding these peptides prefcrentially bound to the LPS of Salmonella family. AWLPWAK-conjugated beads absorbed Salmonella enteritidis from solution and showed a preference for S. enteritidis over Escherichia coli. In summary, this study shows for the first time that a peptide screened from phage displays of combinatorial peptide libraries can be synthesized on beads and be used practically to concentrate bacterial cells from solution. (C) 2005 Elsevier Inc. All rights reserved.
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