Real-time quantitative analysis of lipid disordering by aurein 1.2 during membrane adsorption, destabilisation and lysis

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 10, 2010, Pages 1977-1986

  Lee, Tzong Hsien ^a   Heng, Christine ^a   Swann, Marcus J ^b   Gehman, John D ^c   Separovic, Frances ^c   Aguilar, Marie Isabel ^a  

^a MONASH UNIVERSITY   (Australia)

^b Farfield Group   (United Kingdom)

^c UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Aurein; Australian amphibian antimicrobial peptides; Dual polarisation interferometry; Lipid peptide interactions; Phospholipid membranes; Supported lipid bilayers

Indexed keywords

AUREIN 1.2; CHOLESTEROL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; LIPID; POLYPEPTIDE ANTIBIOTIC AGENT; SILICON; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; AUREIN 1.2 PEPTIDE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; LIPID BILAYER; MEMBRANE LIPID; PHOSPHATIDYLGLYCEROL; PROTEIN BINDING;

ADSORPTION KINETICS; ARTICLE; BIREFRINGENCE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ESCHERICHIA COLI; INTERFEROMETRY; LIPID BILAYER; LYSIS; MEMBRANE BINDING; MEMBRANE STABILIZATION; MEMBRANE STRUCTURE; MICELLIZATION; MOLECULAR MECHANICS; NONHUMAN; PHOSPHOLIPID MEMBRANE; POLARIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN LIPID INTERACTION; QUANTITATIVE ANALYSIS; ADSORPTION; ALGORITHM; ANIMAL; CELL MEMBRANE; CHEMICAL MODEL; CHEMISTRY; METABOLISM; PROCEDURES; TIME;

ADSORPTION; ALGORITHMS; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; ESCHERICHIA COLI; INTERFEROMETRY; LIPID BILAYERS; MEMBRANE LIPIDS; MODELS, CHEMICAL; PHOSPHATIDYLGLYCEROLS; PROTEIN BINDING; TIME FACTORS;

AMPHIBIA; ESCHERICHIA COLI;

EID: 77955658948     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.06.023     Document Type: Article

References (49)

1. Heymann D.L. Resistance to anti-infective drugs and the threat to public health. Cell 2006, 124:671-675.
2. Levy S.B., Marshall B. Antibacterial resistance worldwide: causes, challenges and responses. Nat. Med. 2004, 10:S122-S129.
3. Taubes G. The bacteria fight back. Science 2008, 321:356-361.
4. Hoskin D.W., Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim. Biophys. Acta 2008, 1778:357-375.
5. Jenssen H., Hamill P., Hancock R.E. Peptide antimicrobial agents. Clin. Microbiol. Rev. 2006, 19:491-511.
6. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
7. Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 2003, 254:197-215.
8. Brown K.L., Hancock R.E. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 2006, 18:24-30.
9. Kruse T., Kristensen H.H. Using antimicrobial host defense peptides as anti-infective and immunomodulatory agents. Expert. Rev. Anti Infect. Ther. 2008, 6:887-895.
10. Mookherjee N., Hancock R.E. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell. Mol. Life Sci. 2007, 64:922-933.
11. Yeaman M.R., Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003, 55:27-55.
12. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1999, 1462:55-70.
13. Hancock R.E., Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 2002, 206:143-149.
14. Mahalka A.K., Kinnunen P.K. Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim. Biophys. Acta 2009, 1788:1600-1609.
15. Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 2005, 3:238-250.
16. Hancock R.E., Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24:1551-1557.
17. Apponyi M.A., Pukala T.L., Brinkworth C.S., Maselli V.M., Bowie J.H., Tyler M.J., Booker G.W., Wallace J.C., Carver J.A., Separovic F., Doyle J., Llewellyn L.E. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. Peptides 2004, 25:1035-1054.
18. Conlon J.M., Kolodziejek J., Nowotny N. Antimicrobial peptides from the skins of North American frogs. Biochim. Biophys. Acta 2009, 1788:1556-1563.
19. Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C., Tyler M.J. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. Eur. J. Biochem. 2000, 267:5330-5341.
20. Dennison S.R., Harris F., Phoenix D.A. The interactions of aurein 1.2 with cancer cell membranes. Biophys. Chem. 2007, 127:78-83.
21. Giacometti A., Cirioni O., Riva A., Kamysz W., Silvestri C., Nadolski P., Della Vittoria A., Lukasiak J., Scalise G. In vitro activity of aurein 1.2 alone and in combination with antibiotics against gram-positive nosocomial cocci. Antimicrob. Agents Chemother. 2007, 51:1494-1496.
22. Kamysz W., Nadolski P., Kedzia A., Cirioni O., Barchiesi F., Giacometti A., Scalise G., Lukasiak J., Okroj M. In vitro activity of synthetic antimicrobial peptides against Candida. Pol. J. Microbiol. 2006, 55:303-307.
23. Fernandez D.I., Gehman J.D., Separovic F. Membrane interactions of antimicrobial peptides from Australian frogs. Biochim. Biophys. Acta 2009, 1788:1630-1638.
24. Marcotte I., Wegener K.L., Lam Y.H., Chia B.C., de Planque M.R., Bowie J.H., Auger M., Separovic F. Interaction of antimicrobial peptides from Australian amphibians with lipid membranes. Chem. Phys. Lipids 2003, 122:107-120.
25. Dennison S.R., Harris F., Phoenix D.A. Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?. Protein Pept. Lett. 2005, 12:27-29.
26. Seto G.W., Marwaha S., Kobewka D.M., Lewis R.N., Separovic F., McElhaney R.N. Interactions of the Australian tree frog antimicrobial peptides aurein 1.2, citropin 1.1 and maculatin 1.1 with lipid model membranes: differential scanning calorimetric and Fourier transform infrared spectroscopic studies. Biochim. Biophys. Acta 2007, 1768:2787-2800.
27. Ambroggio E.E., Separovic F., Bowie J.H., Fidelio G.D., Bagatolli L.A. Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein. Biophys. J. 2005, 89:1874-1881.
28. Mechler A., Praporski S., Atmuri K., Boland M., Separovic F., Martin L.L. Specific and selective peptide-membrane interactions revealed using quartz crystal microbalance. Biophys. J. 2007, 93:3907-3916.
29. Gehman J.D., Luc F., Hall K., Lee T.H., Boland M.P., Pukala T.L., Bowie J.H., Aguilar M.I., Separovic F. Effect of antimicrobial peptides from Australian tree frogs on anionic phospholipid membranes. Biochemistry 2008, 47:8557-8565.
30. Mashaghi A., Swann M., Popplewell J., Textor M., Reimhult E. Optical anisotropy of supported lipid structures probed by waveguide spectroscopy and its application to study of supported lipid bilayer formation kinetics. Anal. Chem. 2008, 80:3666-3676.
31. Popplewell J.F., Swann M.J., Freeman N.J., McDonnell C., Ford R.C. Quantifying the effects of melittin on liposomes. Biochim. Biophys. Acta 2007, 1768:13-20.
32. Terry C.J., Popplewell J.F., Swann M.J., Freeman N.J., Fernig D.G. Characterisation of membrane mimetics on a dual polarisation interferometer. Biosens. Bioelectron. 2006, 22:627-632.
33. Salamon Z., Tollin G. Optical anisotropy in lipid bilayer membranes: coupled plasmon-waveguide resonance measurements of molecular orientation, polarizability, and shape. Biophys. J. 2001, 80:1557-1567.
34. Ramsden J.J. Molecular orientation in lipid bilayers. Phil. Mag. B 1999, 79:381-386.
35. Mishima K. Birefringence studies on effects of additives on bilayer lipid membranes 2006.
36. den Engelsen D. Optical anisotropy in ordered systems of lipids. Surf. Sci. 1976, 56:272-280.
37. Lee T.H., Hall K.N., Swann M.J., Popplewell J.F., Unabia S., Park Y., Hahm K.S., Aguilar M.I. The membrane insertion of helical antimicrobial peptides from the N-terminus of Helicobacter pylori ribosomal protein L1. Biochim. Biophys. Acta 2010, 1798:544-557.
38. Salamon Z., Lindblom G., Tollin G. Plasmon-waveguide resonance and impedance spectroscopy studies of the interaction between penetratin and supported lipid bilayer membranes. Biophys. J. 2003, 84:1796-1807.
39. de Feijter F.N., Benjamins J., Veer F.A. Ellipsometry as a tool to study the adsorption behaviour of synthetic and biopolymers at the air-water interface. Biopolymers 1978, 17:1759-1772.
40. Sonesson A.W., Callisen T.H., Brismar H., Elofsson U.M. A comparison between dual polarization interferometry (DPI) and surface plasmon resonance (SPR) for protein adsorption studies. Colloids Surf. B Biointerfaces 2007, 54:236-240.
41. Horvath R., Ramsden J. Quasi-isotropic analysis of anisotropic thin films on optical waveguides. Langmuir 2007, 23:9330-9334.
42. Johnson S.J., Bayerl T.M., McDermott D.C., Adam G.W., Rennie A.R., Thomas R.K., Sackmann E. Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons. Biophys. J. 1991, 59:289-294.
43. Kucerka N., Nagle J.F., Sachs J.N., Feller S.E., Pencer J., Jackson A., Katsaras J. Lipid bilayer structure determined by the simultaneous analysis of neutron and X-ray scattering data. Biophys. J. 2008, 95:2356-2367.
44. Nagle J.F., Tristram-Nagle S. Structure of lipid bilayers. Biochim. Biophys. Acta 2000, 1469:159-195.
45. Merz C., Knoll W., Textor M., Reimhult E. Formation of supported bacterial lipid membrane mimics. Biointerphases 2008, 3:FA41-FA50.
46. Balla M.S., Bowie J.H., Separovic F. Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes. Eur. Biophys. J. 2004, 33:109-116.
47. Domanov Y.A., Kinnunen P.K. Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayers. Biophys. J. 2006, 91:4427-4439.
48. Fernandez D.I., Gehman J.D., Separovic F. Membrane interactions of antimicrobial peptides from Australian frogs. Biochim. Biophys. Acta 2009, 1788:1630-1638.
49. Tristram-Nagle S., Liu Y., Legleiter J., Nagle J.F. Structure of gel phase DMPC determined by X-ray diffraction. Biophys. J. 2002, 83:3324-3335.