PEPTIDES INHIBIT COMPLEXATION OF THE BACTERIAL CHAPERONE PAPD AND REVEAL POTENTIAL TO BLOCK ASSEMBLY OF VIRULENCE-ASSOCIATED PILI

Authors
FLEMMER K XU Z PINKNER JS HULTGREN SJ KIHLBERG J
Citation
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
Citations number
16
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
5
Issue
9
Year of publication
1995
Pages
927 - 932
Database
ISI
SICI code
0960-894X(1995)5:9<927:PICOTB>2.0.ZU;2-4
Abstract
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.