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

Biochem Biophys Res Commun. 2005 Apr 1;329(1):312-7. doi: 10.1016/j.bbrc.2005.01.137.

Abstract

The selection of identical or highly homologous peptides from phage display combinatorial peptide libraries has been unsuccessful in biopanning 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 preferentially 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophages / metabolism
  • Biochemistry / methods*
  • Enzyme-Linked Immunosorbent Assay
  • Epoxy Resins / chemistry*
  • Escherichia coli / metabolism
  • Immunoassay
  • Lipopolysaccharides* / chemistry
  • Microscopy, Fluorescence
  • Peptide Library*
  • Peptides / chemistry*
  • Polysaccharides / chemistry
  • Protein Binding
  • Salmonella enteritidis / chemistry
  • Salmonella enteritidis / metabolism
  • Surface Plasmon Resonance

Substances

  • Epoxy Resins
  • Lipopolysaccharides
  • Peptide Library
  • Peptides
  • Polysaccharides