Interfacial properties and structural analysis of the antimicrobial peptide NK-2

Journal of Peptide Science

Volumn 14, Issue 4, 2008, Pages 510-517

  Olak, Claudia ^a   Muenter, Annabel ^a   Andrä, Jörg ^b   Brezesinski, Gerald ^a  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

^b RESEARCH CENTER BORSTEL   (Germany)

Author keywords

Adsorption behavior; Antimicrobial peptides; CD; IRRAS; X ray reflectivity

Indexed keywords

BUFFER; DODECYL SULFATE SODIUM; PEPTIDE NK 2; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; WATER;

ALPHA HELIX; ANTIMICROBIAL ACTIVITY; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CRITICAL MICELLE CONCENTRATION; DRUG ADSORPTION; DRUG STRUCTURE; INFRARED SPECTROSCOPY; INTERMETHOD COMPARISON; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; X RAY ANALYSIS;

AIR; ANTIMICROBIAL CATIONIC PEPTIDES; BUFFERS; CIRCULAR DICHROISM; MICELLES; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, INFRARED; SURFACE PROPERTIES; TRIFLUOROETHANOL; WATER; X-RAYS;

EID: 42149126617     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.954     Document Type: Article

References (37)

1. Bevins CL, Zasloff M. Peptides from Frog-Skin. Annu. Rev. Biochem. 1990; 59: 395-414.
2. Boman HG. Peptide antibiotics and their role in innate immunity. Ann. Rev. Immunol. 1995; 13: 61-92.
3. Broekaert WF, Cammue BPA, DeBolle MFC, Thevissen K, DeSamblanx GW, Osborn RW. Antimicrobial peptides from plants. Crit. Rev. Plant Sci. 1997; 16: 297-323.
4. Hancock REW, Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998; 16: 82-88.
5. Katz E, Demain AL. Peptide antibiotics of bacillus - chemistry, biogenesis, and possible functions. Bacteriol. Rev. 1977; 41: 449-474.
6. White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 1995; 5: 521-527.
7. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
8. Matsuzaki K, Sugishita K, Fujii N, Miyajima K. Molecular-basis for membrane selectivity of an antimicrobial peptide, magainin-2. Biochemistry 1995; 34: 3423-3429.
9. Schröder-Borm H, Willumeit R, Brandenburg K, Andrä J. Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin. Biochim. Biophys. Acta 2003; 1612: 164-171.
10. Piers KL, Brown MH, Hancock REW. Improvement of outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification. Antimicrob. Agents Chemother. 1994; 38: 2311-2316.
11. Andersson M, Gunne H, Agerberth B, Boman A, Bergman T, Sillard R, Jornvall H, Mutt V, Olsson B, Wigzell H, Dagerlind A, Boman HG, Gudmundsson GH. Nk-lysin, a novel effector peptide of cytotoxic T-cells and Nk-cells - structure and cDNA cloning of the porcine form, induction by interleukin-2, antibacterial and antitumor-activity. Embo J. 1995; 14: 1615-1625.
12. Liepinsh E, Andersson M, Ruysschaert JM, Otting G. Saposin fold revealed by the NMR structure of NK-lysin. Nat. Struct. Biol. 1997; 4: 793-795.
13. Andrä J, Leippe M. Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin. Med. Microbiol. Immunol. 1999; 188: 117-124.
14. Andrä J, Monreal D, de Tejada GM, Olak C, Brezesinski G, Gomez SS, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against gram-negative pathogens. J. Biol. Chem. 2007; 282: 14719-14728.
15. Jacobs T, Bruhn H, Gaworski I, Fleischer B, Leippe M. NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi. Antimicrob. Agents Chemother. 2003; 47: 607-613.
16. Schröder-Borm H, Bakalova R, Andrä J. The NK-lysin derived peptide NK-2 preferentially kills cancer cells with increased surface levels of negatively charged phosphatidylserine. FEBS Lett. 2005; 579: 6128-6134.
17. Willumeit R, Kumpugdee M, Funari SS, Lohner K, Navas BP, Brandenburg K, Linser S, Andra J. Structural rearrangement of model membranes by the peptide antibiotic NK-2. Biochim. Biophys. Acta 2005; 1669: 125-134.
18. Andrä J, Koch MHJ, Bartels R, Brandenberg K. Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin. Antimicrob. Agents Chemother. 2004; 48: 1593-1599.
19. Maget-Dana R. The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes. Biochim. Biophys. Acta 1999; 1462: 109-140.
20. Greenfield NJ. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 1996; 235: 1-10.
21. Provencher SW, Glockner J. Estimation of globular protein secondary structure from circular-dichroism. Biochem. 1981; 20: 33-37.
22. Sreerama N, Venyaminov SY, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 2000; 267: 243-251.
23. Flach CR, Gericke A, Mendelsohn R. Quantitative determination of molecular chain tilt angles in monolayer films at the air/water interface: Infrared reflection/absorption spectroscopy of behenic acid methyl ester. J. Phys. Chem. B 1997; 101: 58-65.
24. Kuzmin VL, Mikhailov AV. Molecular theory of light-reflection and the applicability limits of a macroscopic approach. Opt Spektrosk. 1981: 51: 691-695.
25. Mendelsohn R, Brauner JW, Gericke, A. External infrared reflection-absorption spectrometry monolayer films at the air-water-interface. Annu. Rev. Phys. Chem. 1995: 46: 305-334.
26. Jensen TR, Balashev K, Bjoernholm T, Kjaer K. Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part II. Surface sensitive synchrotron X-ray scattering. Biochimie. 2001; 83: 399-408.
27. Kaganer VM, Brezesinski G, Möhwald H, Howes PB, Kjaer K. Positional order in Langmuir monolayers: an x-ray diffraction study. Phys. Rev. E 1999; 59: 2141-2152.
28. Rietz R, Rettig W, Brezesinski G, Bouwman WG, Kjaer K, Möhwald H. Monolayer behaviour of chiral compounds at the air-water interface: 4-hexadecyloxy-butarie-1,2-diol. Thin Solid Films 1996; 285: 211-215.
29. Blaudez D, Turlet JM, Dufourcq J, Bard D, Buffeteau T, Desbat B. Investigations at the air/water interface using polarization modulation IR spectroscopy. J. Chem. Soc., Faraday Trans. 1996; 92: 525-530.
30. Bringezu F, Majerowicz M, Maltseva E, Wen S, Brezesinski G, Waring AJ. Penetration of the antimicrobial peptide dicynthaurin into phospholipid monolayers at the liquid-air interface. ChemBioChem 2007; 8: 1038-1047.
31. Meister A, Kerth A, Blume A. Interaction of sodium dodecyl sulfate with dimyristoyl-sn-glycero-3-phosphocholine monolayers studied by infrared reflection absorption spectroscopy. A new method for the determination of surface partition coefficients. J. Phys. Chem. B 2004; 108: 8371-8378.
32. 2O) Solutions. 3. Estimation of the protein secondary structure. Biopolymers 1990; 30: 1273-1280.
33. Buffeteau T, Le Calvez E, Castano S, Desbat B, Blaudez D, Dufourcq J. Anisotropic optical constants of alpha-helix and beta-sheet secondary structures in the infrared. J. Phys. Chem. B 2000; 104: 4537-4544.
34. Dyck M, Kerth A, Blume A, Losche M. Interaction of the neurotransmitter, neuropeptide Y, with phospholipid membranes: infrared spectroscopic characterization at the air/water interface. J. Phys. Chem. B 2006; 110: 22152-22159.
35. Ambroggio EE, Separovic F, Bowie J, Fidelio GD. Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin. Biochim. Biophys. Acta 2004; 1664: 31-37.
36. Vie V, Van Mau N, Chaloin L, Lesniewska E, Le Grimellec C, Heitz F. Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and Fourier transform infrared analyses. Biophys. J. 2000; 78: 846-856.
37. Zagrovic B, Jayachandran G, Millett IS, Doniach S, Pande VS. How large is an alpha-helix? Studies of the radii of gyration of helical peptides by small-angle X-ray scattering and molecular dynamics. J. Mol. Biol. 2005; 353: 232-241.