Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide

Antimicrobial Agents and Chemotherapy

Volumn 48, Issue 6, 2004, Pages 2190-2198

  Chapple, Daniel S ^a   Hussain, Rohanah ^a   Joannou, Christopher L ^a   Hancock, Robert E W ^c   Odell, Edward ^b   Evans, Robert W ^a   Siligardi, Giuliano ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b GUY S HOSPITAL   (United Kingdom)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

1 N PHENYLNAPHTHYLAMINE; BACTERIUM LIPOPOLYSACCHARIDE; HLP 2 PROTEIN; HLP 6 PROTEIN; LACTOFERRIN; LIGAND; METHIONINE; NAPHTHALENE DERIVATIVE; PEPTIDE DERIVATIVE; PHENYL GROUP; POLYMYXIN B; PROLINE; PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ANTIBACTERIAL ACTIVITY; ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL OUTER MEMBRANE; BACTERICIDAL ACTIVITY; BETA SHEET; BINDING AFFINITY; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONCENTRATION TIME EFFECT RESPONSE; ESCHERICHIA COLI; ESCHERICHIA COLI SEROTYPE O111; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE;

CIRCULAR DICHROISM; COLONY COUNT, MICROBIAL; ESCHERICHIA COLI; LACTOFERRIN; LIPOPOLYSACCHARIDES; MEMBRANES; MODELS, MOLECULAR; PEPTIDES; PERMEABILITY; SPECTROMETRY, FLUORESCENCE;

EID: 2542460301     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.48.6.2190-2198.2004     Document Type: Article

References (25)

1. Bello, T., H. R. Bello, and E. Granados. 1982. Conformation and aggregation of melittin: dependence on pH and concentration. Biochemistry 21:461-465.
2. Bevins, C. 1994. Antimicrobial peptides as agents of mucosal immunity. Ciba Found. Symp. 186:250-269.
3. Boman, H. G. 1995. Peptide antibiotics and their role in innate immmunity. Annu. Rev. Immunol. 13:61-92.
4. Brock, J. H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the new-born infant. Arch. Child. Dis. 55:417-421.
5. Chapple, D. S., D. J. Mason, C. L. Joannou, E. W. Odell, V. Gant, and R. W. Evans. 1998. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherschia coli serotype O111. Infect. Immun. 66:2434-2440.
6. Chapple, D. S., C. L. Joannou, D. J. Mason, J. K. Shergill, E. W. Odell, V. Gant, and R. W. Evans. 1998. A helical region on human lactoferrin - its role in antibacterial pathogenesis. Adv. Exp. Med. Biol. 443:215-220.
7. Falla, T. J., N. Karunaratne, and R. E. W. Hancock. 1996. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271:19298-19303.
8. Fidai, S., S. W. Farmer, and R. E. W. Hancock. 1997. Interactions of cationic peptides with bacterial membranes. Methods Mol. Biol. 78:187-204.
9. Hancock, R. E. W., and G. Diamond. 2000. Cationic antimicrobial peptides: a major element in mammalian innate immune defences against infection. Trends Microbiol. 8:402-410.
10. Hancock, R. E. W., and D. S. Chapple. 1999. Antibiotic peptides. Antimicrob. Agents Chemother. 43:215-220.
11. Hancock, R. E. W., and R. Lehrer. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88.
12. Hancock, R. E. W. 1997. Peptide antibiotics. Lancet 349:418-422.
13. Hancock, R. E. W., C. Egli, and N. Karunaratne. 1994. Molecular organization and structural role of outer membrane macromolecules, p. 263-279. In J. M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell envelope. Elsevier Science Publishers BV, Amsterdam, The Netherlands.
14. Houston, M. E., L. H. Kondejewski, D. N. Karunaratne, M. Gough, S. Fidai, R. S. Hodges, and R. E. W. Hancock. 1998. Influence of preformed α-helix and α-helix induction on the activity of cationic antimicrobial peptides. J. Pept. Res. 52:81-88.
15. Hwang, P. M., N. Zhou, X. Shan, C. H. Arrowsmith, and H. J. Vogel. 1998. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37:4288-4298.
16. Jelokhani-Niaraki, M., L. H. Kondejewski, S. W. Farmer, R. E. W. Hancock, C. M. Kay, and R. S. Hodges. 2000. Diastereoisomeric analogues of gramicidin S: structure, biological activity and interaction with lipid bilayers. Biochem. J. 349:747-755.
17. Kang, J. H., K. L. Lee, K. L. Kim, and K. S. Hahan. 1996. Structure-biological activity relationship of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Pept. Protein Res. 48:357-363.
18. Kuwata, H., T. Yip, K. Yamauchi, S. Teraguchi, H. Hayasawa, M. Tomita, and T. Hutchens. 1998. The survival of ingested lactoferrin in the gastrointestinal tract of adult mice. Biochem. J. 334:321-323.
19. Loh, B., C. Grant, and R. E. W. Hancock. 1984. Use of fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 26:546-551.
20. Moore, R. A., N. C. Bates, and R. E. W. Hancock. 1986. Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin. Antimicrob. Agents Chemother. 29:496-500.
21. Odell, E. W., R. Sarra, M. Foxworthy, D. S. Chapple, and R. W. Evans. 1996. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382:175-178.
22. Oren, Z., J. C. Lerman, G. H. Gudmundsson, B. Agerberth, and Y. Shai. 1999. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341:501-513.
23. Sawyer, J. G., N. L. Martin, and R. E. W. Hancock. 1988. Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa. Infect. Immun. 56:693-698.
24. Vogel, H. J., and F. Jahnig. 1986. The structure of melittin in membranes. Biophys. J. 50:573-582.
25. Zhang, L., R. Benz, and R. E. W. Hancock. 1999. Influence of proline residues on the antibacterial and synergistic activities of α-helical peptides. Biochemistry 38:8102-8111.