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| - Multivariate Design, Synthesis, and Biological Evaluation of Peptide Inhibitorsof FimC/FimH Protein−Protein Interactions in Uropathogenic Escherichia coli
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| - A peptide library targeting protein−protein interactions crucial for pilus assembly in Gramnegative bacteria has been designed using statistical molecular design. A nonamer peptidescaffold was used, with seven positions being varied. The selection was performed in the buildingblock space, and previously known structure−activity data were included in the designprocedure. This resulted in a heavily reduced library consisting of 32 peptides which wasprepared by solid-phase synthesis. The ability of the peptides to inhibit the protein−proteininteraction between the periplasmic chaperone FimC and the pilus adhesin FimH was thendetermined in an ELISA. Novel peptides with the capability to inhibit the FimC/FimH protein−protein interaction to the same extent as the native FimC peptides were discovered. MultivariateQSAR studies of the response in the ELISA gave valuable information on the properties ofamino acids which were preferred at the seven positions in the nonamer scaffold. Thisinformation can be used in attempts to develop optimized peptides and peptidomimetics thatinhibit pilus assembly in pathogenic bacteria.
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