Binding of peptides in solution by the Escherichia coli chaperone PapD as revealed using an inhibition ELISA and NMR spectroscopy

Katarina Flemmer Karlsson, Björn Walse, Torbjörn Drakenberg, Sarbari Roy, Karl Erik Bergquist, Jerome S. Pinkner, Scott J. Hultgren, Jan Kihlberg

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

PapD is the prototype member of a family of periplasmic chaperones which are required for assembly of virulence associated pili in pathogenic, gram-negative bacteria. In the present investigation, an ELISA has been developed for evaluation of compounds as inhibitors of PapD. Synthetic peptides, including an octamer, derived from the C-terminus of the pilus adhesin PapG were able to inhibit PapD in the ELISA. Evaluation of a panel of octapeptides in the ELISA, in combination with NMR studies, showed that the peptides were bound as extended β-strands by PapD in aqueous solution. The PapD-peptide complex was stabilized by backbone to backbone hydrogen bonds and interactions involving three hydrophobic peptide side chains. This structural information, together with previous crystal structure data, provides a starting point in efforts to design and synthesize compounds which bind to chaperones and interfere with pilus assembly in pathogenic bacteria. Copyright (C) 1997 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)2085-2101
Number of pages17
JournalBioorganic and Medicinal Chemistry
Volume6
Issue number11
DOIs
StatePublished - Nov 1 1998

Keywords

  • Chaperone
  • ELISA
  • NMR spectroscopy
  • Peptide
  • Pili
  • Structure-activity

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