K. Flemmer et al., PEPTIDES INHIBIT COMPLEXATION OF THE BACTERIAL CHAPERONE PAPD AND REVEAL POTENTIAL TO BLOCK ASSEMBLY OF VIRULENCE-ASSOCIATED PILI, Bioorganic & medicinal chemistry letters, 5(9), 1995, pp. 927-932
Peptides as small as octamers were found to inhibit protein-protein co
mplex formation between the PapD chaperone and the pilus adhesin PapG.
The intermolecular hydrogen bonding pattern in the crystalline comple
x of PapD with a peptide from PapG was revealed to be important also f
or complex formation in solution. The role of the peptide side chains
was indicated to be slightly different as compared to in the crystal.