Oxidized phospholipids as potential molecular targets for antimicrobial peptides

Biochimica et Biophysica Acta - Biomembranes

Volumn 1778, Issue 10, 2008, Pages 2041-2050

  Mattila, Juha Pekka ^a   Sabatini, Karen ^a   Kinnunen, Paavo K J ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Monolayer penetration; Peptide lipid interactions; Reactive oxygen species; Tryptophan fluorescence

Indexed keywords

1 PALMITOYL 2 (9' OXONONANOYL) GLYCERO 3 PHOSPHOCHOLINE; 1 PALMITOYL 2 AZELAOYLGLYCERO 3 PHOSPHOCHOLINE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; INDOLICIDIN; METHOXYAMINE; PHOSPHATIDYLGLYCEROL; PHOSPHOLIPID; PHOSPHOLIPID DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; SCHIFF BASE; TEMPORIN B; TEMPORIN L; UNCLASSIFIED DRUG;

ARTICLE; BILAYER MEMBRANE; BINDING ASSAY; DRUG STRUCTURE; DRUG TARGETING; FLUORESCENCE SPECTROSCOPY; IONIC STRENGTH; LANGMUIR BLODGETT FILM; LIPID MONOLAYER; LIPID OXIDATION; MEMBRANE BINDING; MEMBRANE MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE;

ANIMALS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; BUFFERS; HUMANS; LIPOSOMES; OXIDATION-REDUCTION; PEPTIDES; PHOSPHOLIPIDS; PROTEINS;

EID: 52049111367     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.03.020     Document Type: Article

References (54)

1. Ganz T., and Lehrer R.I. Antimicrobial peptides of vertebrates. Curr. Opin. Immunol. 10 (1998) 41-44
2. Hancock R.E., and Scott M.G. The role of antimicrobial peptides in animal defences. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 8856-8861
3. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
4. http://aps.unmc.edu/AP/main.php.
5. He J., Eckert R., Pharm T., Simanian M.D., Hu C., Yarbrough D.K., Qi F., Anderson M.H., and Shi W. Novel synthetic antimicrobial peptides against Streptococcus mutans. Antimicrob. Agents Chemother. 51 (2007) 1351-1358
6. Hancock R.E., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends. Biotechnol. 16 (1998) 82-88
7. Bechinger B., and Lohner K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006) 1529-1539
8. Zhao H., Jutila A., Nurminen T., Wickström S.A., Keski-Oja J., and Kinnunen P.K.J. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 44 (2005) 2857-2863
9. Zhao H., Sood R., Jutila A., Bose S., Fimland G., Nissen-Meyer J., and Kinnunen P.K.J. Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action. Biochim. Biophys. Acta 1758 (2006) 1461-1474
10. Bowdish D.M., Davidson D.J., and Hancock R.E. A re-evaluation of the role of host defence peptides in mammalian immunity. Curr. Prot. Peptide Sci. 6 (2005) 35-51
11. Mookherjee N., and Hancock R.E. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell. Mol. Life Sci. 64 (2007) 922-933
12. Sood R., Domanov Y., Pietiäinen M., Kontinen V.P., and Kinnunen P.K.J. Binding of LL-37 to model biomembranes: insight into target vs host cell recognition. Biochim. Biophys. Acta 1778 (2008) 983-996
13. Zhao H., Rinaldi A.C., Di Giulio A., Simmaco M., and Kinnunen P.K.J. Interaction of the antimicrobial peptides temporins with model biomembranes. Comparison of Temporins B and L. Biochemistry 41 (2002) 4425-4436
14. Zhao H., and Kinnunen P.K.J. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 277 (2002) 25170-25177
15. Mangoni M.L., Rinaldi A.C., Di Giulio A., Mignogna G., Bozzi A., Barra D., and Simmaco M. Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. Eur. J. Biochem. 267 (2000) 1447-1454
16. Rozek A., Friedrich C.L., and Hancock R.E. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39 (2000) 15765-15774
17. Malm J., Sorensen O., Persson T., Frohm-Nilsson M., Johansson B., Bjartell A., Lilja H., Stahle-Backdahl M., Borregaard N., and Egesten A. The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa. Infect. Immun. 683 (2000) 4297-4302
18. Hase K., Eckmann L., Leopard J.D., Varki N., and Kagnoff M.F. Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. Infect. Immun. 70 (2002) 953-963
19. Bowdish D.M., Davidson D.J., Lau Y.E., Lee K., Scott M.G., and Hancock R.E. Impact of LL-37 on anti-infective immunity. J. Leukoc. Biol. 77 (2005) 451-459
20. Oren Z., Lerman J.C., Gudmundsson G.H., Agerberth B., and Shai Y. 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 (1999) 501-513
21. Henzler Wildman K.A., Lee D.K., and Ramamoorthy A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 42 (2003) 6545-6558
22. Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
23. Zhao H., Mattila J.-P., Holopainen J.M., and Kinnunen P.K.J. Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin. Biophys. J. 81 (2001) 2979-2991
24. Fruhwirth G.O., Loidl A., and Hermetter A. Oxidized phospholipids: from molecular properties to disease. Biochim. Biophys. Acta 1772 (2007) 718-736
25. Sabatini K., Mattila J.-P., Megli F.M., and Kinnunen P.K.J. Characterization of two oxidatively modified phospholipids in mixed monolayers with DPPC. Biophys. J. 90 (2006) 4488-4499
26. Verger R., and Pattus F. Spreading of membranes at the air/water interface. Chem. Phys. Lipids 16 (1976) 285-291
27. Brockman H. Lipid monolayers: why to use half of a membrane to characterize protein-membrane interactions?. Curr. Opin. Struck. Biol. 9 (1999) 438-443
28. Berger N., Sachse A., Bender J., Schubert R., and Brandl M. Filter extrusion of liposomes using different devices: comparison of liposome size, encapsulation efficiency, and process characteristics. Int. J. Pharm. 223 (2001) 55-68
29. Mattila J.-P., Sabatini K., and Kinnunen P.K.J. Oxidized phospholipids as potential novel drug targets. Biophys. J. 93 (2007) 3105-3112
30. De Kroon A.I.P.M., Soekarjo M.W., De Gier J., and De Kruijff B. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on Tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 29 (1990) 8229-8240
31. Eftink M.R., and Ghiron C.A. Fluorescence quenching of indole and model micelle systems. J. Phys. Chem 80 (1976) 486-493
32. Lamy-Freund M.T., and Riske K.A. The peculiar thermo-structural behavior of the anionic lipid DMPG. Chem. Phys. Lipids 122 (2003) 19-32
33. Breukink E., van Kraaij C., van Dalen A., Demel R.A., Siezen R.J., de Kruijff B., and Kuipers O.P. The orientation of nisin in membrane. Biochemistry 37 (1998) 8153-8162
34. Surewicz W.K., and Epand R.M. Role of peptide in lipid-peptide interactions: a fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles. Biochemistry 23 (1984) 6072-6077
35. Cowgill R.W. Fluorescence and protein structure. X. Reappraisal of solvent and structural effects. Biochim. Biophys. Acta 133 (1967) 6-18
36. Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
37. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipids bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
38. Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
39. Demel R.A., van Kessel W.S.G., Zwaal R.F., Roelofsen B., and van Deenen L.L. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta 406 (1975) 97-107
40. Shan S.O., Loh S., and Herschlag D. The energetics of hydrogen bonds in model systems: implications for enzymatic catalysis. Science 272 (1996) 97-101
41. Ahmed Z., Ravandi A., Maguire G.F., Kuksis A., and Connelly P.W. Formation of apolipoprotein AI-phosphatidylcholine core aldehyde Schiff base adducts promotes uptake by THP-1 macrophages. Cardiovasc. Res. Jun. 58 (2003) 712-720
42. Bieschke J., Zhang Q., Bosco D.A., Lerner R.A., Powers E.T., Wentworth Jr. P., and Kelly J.W. Small molecule oxidation products trigger disease-associated protein misfolding. Acc. Chem. Res. 39 (2006) 611-619
43. Steinbrecher U.P. Oxidation of human low density lipoprotein results in derivatization of lysine residues of Apolipoprotein B by lipid peroxide decomposition products. J. Biol. Chem. 262 (1987) 3603-3608
44. Kurvinen J.-P., Kuksis A., Ravandi A., Sjövall O., and Kallio H. Rapid complexing of oxoacylglycerols with amino acids, peptides and aminophospholipids. Lipids 34 (1999) 299-305
45. Halliwell B., and Gutteridge J.M. Role of free radicals and catalytic metal ions in human disease: an overview. Methods. Enzymol 186 (1990) 1-85
46. Gago-Dominguez M., Castelao J.E., Yuan J.M., Ross R.K., and Yu M.C. Lipid peroxidation: a novel and unifying concept of the etiology of renal cell carcinoma (United States). Cancer Causes Control 13 (2002) 287-293
47. Cejas P., Casado E., Belda-Iniesta C., De Castro J., Espinosa E., Redondo A., Sereno M., Garcia-Cabezas M.A., Vara J.A.F., Domi{dotless}nguez-Caceres A., Perona R., and Gonzalez-Baron M. Implication of oxidative stress and cell membrane lipid peroxidation in human cancer (Spain). Cancer Causes Control 15 (2004) 707-719
48. Berliner J.A., and Heinecke J.W. The role of oxidized lipoproteins in atherogenesis. Free Radic. Biol. Med 20 (1996) 707-727
49. Davies S.S., Pontsler A.V., Marathe G.K., Harrison K.A., Murphy R.C., Hinshaw J.C., Prestwich G.D., Hilaire A.S., Prescott S.M., Zimmerman G.A., and McIntyre T.M. Oxidized alkyl phospholipids are specific, high affinity peroxisome proliferator-activated receptor gamma ligands and agonists. J. Biol. Chem. 276 (2001) 16015-16023
50. Ahmed Z., Ravandi A., Maguire G.F., Emili A., Draganov D., La Du B.N., Kuksis A., and Connelly P.W. Apolipoprotein A-I promotes the formation of phosphatidylcholine core aldehydes that are hydrolyzed by paraoxonase (PON-1) during high density lipoprotein oxidation with a peroxynitrate donor. J. Biol. Chem. 276 (2001) 24473-24481
51. Koppaka V., Paul C., Murray I.V., and Axelsen P.H. Early synergy between Abeta42 and oxidatively damaged membranes in promoting amyloid fibril formation by Abeta40. J. Biol. Chem. 278 (2003) 36277-36284
52. Koppaka V., and Axelsen P.H. Accelerated accumulation of amyloid beta proteins on oxidatively damaged lipid membranes. Biochemistry 32 (2000) 10011-10016
53. Mayer-Scholl A., Averhoff P., and Zychlinsky A. How do neutrophils and pathogens interact?. Curr. Opin. Microbiol. 7 (2004) 62-66
54. Roos D., and Winterbourn C.C. Immunology. Lethal weapons. Science 296 (2002) 669-671