Screening of LPS-specific peptides from a phage display library using epoxy beads
- Authors
- Kim, YG; Lee, CS; Chung, WJ; Kim, E; Shin, DS; Rhim, JH; Lee, YS; Kim, BG; Chung, 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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