Interactions of an anionic antimicrobial peptide with Staphylococcus aureus membranes

Biochemical and Biophysical Research Communications

Volumn 347, Issue 4, 2006, Pages 1006-1010

  Dennison, Sarah R ^a   Howe, Jörg ^b   Morton, Leslie H G ^a   Brandenburg, Klaus ^b   Harris, Frederick ^a   Phoenix, David A ^a  

^a UNIVERSITY OF CENTRAL LANCASHIRE   (United Kingdom)

^b RESEARCH CENTER BORSTEL   (Germany)

Author keywords

Anionic helical peptide; Antimicrobial; Fourier transform infrared spectroscopy; Langmuir Blodgett; Lipid extract; Monolayer; Staphylococcus aureus membrane

Indexed keywords

GLYCYLGLUTAMYLGLUTAMINYLGLYCYLALANYLLEUCYLALANYLGLUTAMINYLPHENYLALANYL GLYCYLGLUTAMYLTRYPTOPHANYLLEUCYL; LIPID; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ALPHA HELIX; ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL MEMBRANE; BACTERICIDAL ACTIVITY; CONTROLLED STUDY; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; INFRARED SPECTROSCOPY; LIPID COMPOSITION; MEMBRANE FLUIDITY; NONHUMAN; PRESSURE; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS; STRUCTURE ACTIVITY RELATION;

ANTI-BACTERIAL AGENTS; CELL MEMBRANE; LIPOSOMES; MEMBRANE LIPIDS; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STAPHYLOCOCCUS AUREUS;

NEGIBACTERIA; POSIBACTERIA; STAPHYLOCOCCUS AUREUS;

EID: 33746332669     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.181     Document Type: Article

References (34)

1. Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 3 (2005) 238-250
2. Dennison S.R., Wallace J., Harris F., and Phoenix D.A. Amphiphilic alpha-helical antimicrobial peptides and their structure/function relationships. Protein Pept. Lett. 12 (2005) 31-39
3. Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
4. I. Zelezetsky, A. Tossi, Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies, Biochim. Biophys. Acta (2006) (in press).
5. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
6. Reddy K.V., Yedery R.D., and Aranha C. Antimicrobial peptides: premises and promises. Int. J. Antimicrob. Agents 24 (2004) 536-547
7. Schroder J.M., and Harder J. Antimicrobial peptides in skin disease. Drug Discov. Today: Ther. Strategies 3 (2006) 93-100
8. Yedery R.D., and Reddy K.V.R. Antimicrobial peptides as microbicidal contraceptives: prophecies for prophylactics-a mini review. Eur. J. Contracept. Reprod. Health Care 10 (2005) 32-42
9. Diamond G. Natures antibiotics: the potential of antimicrobial peptides as new drugs. Biologist (London) 48 (2001) 209-212
10. Nizet V. Antimicrobial peptide resistance mechanisms of human bacterial pathogens. Curr. Issues Mol. Biol. 8 (2006) 11-26
11. Peschel A. How do bacteria resist human antimicrobial peptides?. Trends Microbiol. 10 (2002) 179-186
12. Perron G.G., Zasloff M., and Bell G. Experimental evolution of resistance to an antimicrobial peptide. Proc. Biol. Sci. 273 (2006) 251-256
13. Lai R., Liu H., Hui Lee W., and Zhang Y. An anionic antimicrobial peptide from toad Bombina maxima. Biochem. Biophys. Res. Commun. 295 (2002) 796-799
14. Marshall S.H., and Arenas G. Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology. Electron. J. Biotechnol. 6 (2003) [online]
15. Nascimento A.C., Fontes W., Sebben A., and Castro M.S. Antimicrobial peptides from anurans skin secretions. Protein Pept. Lett. 10 (2003) 227-238
16. Goumon Y., Strub J.M., Moniatte M., Nullans G., Poteur L., Hubert P., Van Dorsselaer A., Aunis D., and Metz-Boutigue M.H. The C-terminal bisphosphorylated proenkephalin-A-(209-237)-peptide from adrenal medullary chromaffin granules possesses antibacterial activity. Eur. J. Biochem. 235 (1996) 516-525
17. Stern A.S., Jones B.N., Shively J.E., Stein S., and Undenfriend S. Two adrenal opioid polypeptides: proposed intermediates in the processing of proenkephalin. Proc. Natl. Acad. Sci. USA 78 (1981) 1962-1966
18. Schittek B., Hipfel R., Sauer B., Bauer J., Kalbacher H., Stevanovic S., Schirle M., Schroeder K., Blin N., Meier F., Rassner G., and Garbe C. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat. Immunol. 2 (2001) 1133-1137
19. Baechle D., Flad T., Cansier A., Steffen H., Schittek B., Tolson J., Herrmann T., Dihazi H., Beck A., Mueller G.A., Mueller M., Stevanovic S., Garbe C., Mueller C.A., and Kalbacher H. Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L. J. Biol. Chem. 281 (2006) 5406-5415
20. Cipakova I., Gasperik J., and Hostinova E. Expression and purification of human antimicrobial peptide, dermcidin, in Escherichia coli. Protein Expr. Purif. 45 (2006) 269-274
21. Lai Y.P., Peng Y.F., Zuo Y., Li J., Huang J., Wang L.F., and Wu Z.R. Functional and structural characterization of recombinant dermcidin-1L, a human antimicrobial peptide. Biochem. Biophys. Res. Commun. 328 (2005) 243-250
22. Lansac G., Dong W., Dubois C.M., Benlarbi N., Afonso C., Fournier I., Salzet M., and Day R. Lipopolysaccharide mediated regulation of neuroendocrine associated proprotein convertases and neuropeptide precursor processing in the rat spleen. J. Neuroimmunol. 171 (2006) 57-71
23. Metz-Boutigue M.H., Kieffer A.E., Goumon Y., and Aunis D. Innate immunity: involvement of new neuropeptides. Trends Microbiol. 11 (2003) 585-592
24. Steffen H., Rieg S., Wiedemann I., Kallbacher H., Peschel A., Garbe C., and Schittek B. Structural requirements and mechanism of antimicrobial activity of dermcidin-derived peptides. Exp. Dermatol. 15 (2006) 204
25. Goumon Y., Lugardon K., Kieffer B., Lefevre J.F., Van Dorsselaer A., Aunis D., and Metz-Boutigue M.H. Characterization of antibacterial COOH-terminal proenkephalin-A-derived peptides (PEAP) in infectious fluids. Importance of enkelytin, the antibacterial PEAP209-237 secreted by stimulated chromaffin cells. J. Biol. Chem. 273 (1998) 29847-29856
26. 1H NMR spectroscopy. J. Biol. Chem. 273 (1998) 33517-33523
27. A. Thomas, R. Brasseur, Tilted peptides: the history, current protein and peptide science (2006) (in press).
28. Dennison S.R., Harris F., and Phoenix D.A. Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?. Protein Pept. Lett. 12 (2005) 27-29
29. S.R. Dennison, L.H.G. Morton, K. Brandenburg, F. Harris, D.A. Phoenix, Investigations into the ability of an oblique α-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide, FEBS (2006) (in press).
30. Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Med. Sci. 37 (1959) 911-917
31. Keller R.C., Killian J.A., and de Kruijff B. Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles. Biochemistry 31 (1992) 1672-1677
32. Brandenburg K., Harris F., Dennison S., Seydel U., and Phoenix D. Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid. Eur. J. Biochem. 269 (2002) 5414-5422
33. Brandenburg K., Kusumoto S., and Seydel U. Conformational studies of synthetic lipid A analogues and partial structures by infrared spectroscopy. Biochim. Biophys. Acta 1329 (1997) 183-201
34. In: Ratledge C., and Wilkinson S.G. (Eds). Microbial Lipids vol. 1 (1988), Academic Press, London