Peptides inhibit complexation of the bacterial chaperone papd and reveal potential to block assembly of virulence associated pili

Peptides as small as octamers were found to inhibit protein-protein complex formation between the PapD chaperone and the pilus adhesin PapG. The intermolecular hydrogen bonding pattern in the crystalline complex of PapD with a peptide from PapG was revealed to be important also for complex formation in solution. The role of the peptide side chains was indicated to be slightly different as compared to in the crystal.