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Volumn 28, Issue 2, 2009, Pages 105-116

New strategies for novel antibiotics: Peptides targeting bacterial cell membranes

Author keywords

Biomembrane mimetics; Cubic phases; Interdigitation; Lipid segregation; Membrane domains

Indexed keywords

ALAMETHICIN; AMIKACIN; BACITRACIN; CHLORAMPHENICOL; CLINDAMYCIN; DAPTOMYCIN; ERYTHROMYCIN; GENTAMICIN; GRAMICIDIN S; LANTIBIOTIC; LIPOSOME; MEMBRANE LIPID; MONOBACTAM; OXAZOLIDINONE DERIVATIVE; PENICILLIN G; PEPTIDE; PHOSPHATIDYLCHOLINE; POLYPEPTIDE ANTIBIOTIC AGENT; QUINOLONE; RIFAMPICIN; RNA POLYMERASE; SPECTINOMYCIN; STREPTOMYCIN; SULFONAMIDE; TETRACYCLINE; TOBRAMYCIN; TRIMETHOPRIM; VANCOMYCIN;

EID: 67650957816     PISSN: 02315882     EISSN: None     Source Type: Journal    
DOI: 10.4149/gpb_2009_02_105     Document Type: Review
Times cited : (167)

References (98)
  • 1
    • 60549086215 scopus 로고    scopus 로고
    • Peptide induced demixing in PG/PE lipid mixtures: A mechanism for the specificity of antimicrobial peptides towards bacterial membranes?
    • doi:10.1016/j.bbamem.2008.11.022
    • Arouri A., Dathe M., Blume A. (2009): Peptide induced demixing in PG/PE lipid mixtures: A mechanism for the specificity of antimicrobial peptides towards bacterial membranes? Biochim. Biophys. Acta 1788, 650-659; doi:10.1016/j.bbamem.2008.11.022
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 650-659
    • Arouri, A.1    Dathe, M.2    Blume, A.3
  • 2
    • 0027727710 scopus 로고
    • Interaction of tertiary amine anesthetics with phosphatidylcholine bilayers
    • doi:10.1007/BFb0118503
    • Balgavý P., Uhríková D., Gallová J., Lohner K., Degovics G. (1993): Interaction of tertiary amine anesthetics with phosphatidylcholine bilayers. Prog. Coll. Polym. Sci. 93, 184-185; doi:10.1007/BFb0118503
    • (1993) Prog. Coll. Polym. Sci. , vol.93 , pp. 184-185
    • Balgavý, P.1    Uhríková, D.2    Gallová, J.3    Lohner, K.4    Degovics, G.5
  • 3
    • 0030581202 scopus 로고    scopus 로고
    • Cut-off effects in biological activities of surfactants
    • doi:10.1016/0001-8686(96)00295-3
    • Balgavý P., Devínsky F. (1996): Cut-off effects in biological activities of surfactants. Adv. Colloid Interface Sci. 66, 23-63; doi:10.1016/0001-8686(96)00295-3
    • (1996) Adv. Colloid Interface Sci. , vol.66 , pp. 23-63
    • Balgavý, P.1    Devínsky, F.2
  • 5
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic antimicrobial peptides
    • doi:10.1016/j.bbamem.2006.07.001
    • Bechinger B., Lohner K. (2006): Detergent-like actions of linear amphipathic antimicrobial peptides. Biochim. Biophys. Acta 1758, 1529-1539; doi:10.1016/j.bbamem.2006.07.001
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 7
    • 0028938736 scopus 로고
    • Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli
    • doi:10.1074/jbc.270.2.732
    • Bogdanov M., Dowhan W. (1995): Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli. J. Biol. Chem. 270, 732-739; doi:10.1074/jbc.270.2.732
    • (1995) J. Biol. Chem. , vol.270 , pp. 732-739
    • Bogdanov, M.1    Dowhan, W.2
  • 8
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • doi:10.1016/0092-8674(91)90154-Q
    • Boman H. G. (1991): Antibacterial peptides: key components needed in immunity. Cell 65, 205-207; doi:10.1016/0092-8674(91)90154-Q
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 9
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • doi:10.1046/j.1365-2796.2003.01228.x
    • Boman H. G. (2003): Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254, 197-215; doi:10.1046/j.1365-2796.2003.01228.x
    • (2003) J. Intern. Med. , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 10
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane
    • DOI 10.1021/bi970008u
    • Breukink E., van Kraaij C., Demel A. R., Peelen T., Siezen R., de Kruijff B., Kuipers O. (1997): The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane. Biochemistry 36, 6968-6976; doi:10.1021/bi970008u (Pubitemid 27258109)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 6968-6976
    • Breukink, E.1    Van Kraaij, C.2    Demel, R.A.3    Siezen, R.J.4    Kuipers, O.P.5    De Kruijff, B.6
  • 12
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • doi:10.1016/S0006-3495(03)75103-75110
    • Chen F. Y., Lee M. T., Huang H. W. (2003): Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84, 3751-3758; doi:10.1016/S0006-3495(03)75103-75110
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 13
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis P. R., de Kruijff B. (1979): Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559, 399-420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 14
    • 0031566307 scopus 로고    scopus 로고
    • Biomembranes. Lipids beyond the bilayer
    • doi:10.1038/386129a0
    • de Kruijff B. (1997): Biomembranes. Lipids beyond the bilayer. Nature 386, 129-130; doi:10.1038/386129a0
    • (1997) Nature , vol.386 , pp. 129-130
    • De Kruijff, B.1
  • 15
    • 0036467404 scopus 로고    scopus 로고
    • General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides
    • doi:10.1016/S0005-2736(01)00429-1
    • Dathe M., Meyer J., Beyermann M., Maul B., Hoischen C., Bienert M. (2002): General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides. Biochim. Biophys. Acta 1558, 171-186; doi:10.1016/S0005-2736(01)00429-1
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 171-186
    • Dathe, M.1    Meyer, J.2    Beyermann, M.3    Maul, B.4    Hoischen, C.5    Bienert, M.6
  • 16
    • 0032581038 scopus 로고    scopus 로고
    • Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane α-helical peptides and gramicidin A
    • doi:10.1021/bi980233r
    • de Planque M. R., Greathouse D. V., Koeppe R. E., Schafer H., Marsh D., Killian J. A. (1998): Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane α-helical peptides and gramicidin A. Biochemistry 37, 9333-9345; doi:10.1021/bi980233r
    • (1998) Biochemistry , vol.37 , pp. 9333-9345
    • De Planque, M.R.1    Greathouse, D.V.2    Koeppe, R.E.3    Schafer, H.4    Marsh, D.5    Killian, J.A.6
  • 17
    • 0025685615 scopus 로고
    • Cut-off effect in antimicrobial activity and in membrane perturbation efficiency of the homologous series of N,N-dimethylalkylamine oxides
    • Devínsky F., Kopecká-Leitmanová A., Šeršeň F., Balgavý P. (1990): Cut-off effect in antimicrobial activity and in membrane perturbation efficiency of the homologous series of N,N-dimethylalkylamine oxides. J. Pharm. Pharmacol. 42, 790-794
    • (1990) J. Pharm. Pharmacol. , vol.42 , pp. 790-794
    • Devínsky, F.1    Kopecká-Leitmanová, A.2    Šeršeň, F.3    Balgavý, P.4
  • 18
    • 0032929807 scopus 로고    scopus 로고
    • Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamine
    • doi:10.1016/S0005-2736(99)00027-9
    • El Jastimi R., Lafleur M. (1999): Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamine. Biochim. Biophys. Acta. 1418, 97-105; doi:10.1016/S0005-2736(99)00027-9
    • (1999) Biochim. Biophys. Acta. , vol.1418 , pp. 97-105
    • El Jastimi, R.1    Lafleur, M.2
  • 19
    • 0345074088 scopus 로고    scopus 로고
    • Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins
    • doi:10.1046/j.1432-1033.2003.03484.x
    • Epand R. F., Umezawa N., Porter E. A., Gellman S. H., Epand R. M. (2003): Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins. Eur. J. Biochem. 270, 1240-1248; doi:10.1046/j.1432-1033.2003.03484.x
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1240-1248
    • Epand, R.F.1    Umezawa, N.2    Porter, E.A.3    Gellman, S.H.4    Epand, R.M.5
  • 20
    • 33748929313 scopus 로고    scopus 로고
    • Role of membrane lipids in the mechanism of bacterial species selective toxicity by two α/β-antimicrobial peptides
    • doi:10.1016/j.bbamem.2006.01.018
    • Epand R. F., Schmitt M. A., Gellman S. H., Epand R. M. (2006): Role of membrane lipids in the mechanism of bacterial species selective toxicity by two α/β-antimicrobial peptides. Biochim. Biophys. Acta 1758, 1343-1350; doi:10.1016/j.bbamem.2006.01.018
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1343-1350
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Epand, R.M.4
  • 21
    • 42749091734 scopus 로고    scopus 로고
    • Dual mechanism of bacterial lethality for a cationic sequence-random copolymer that mimics host-defense antimicrobial peptides
    • doi:10.1016/j.jmb.2008.03.047
    • Epand R. F., Mowery B. P., Lee S. E., Stahl S.S., Lehrer R. I., Gellman S. H., Epand R. M. (2008a): Dual mechanism of bacterial lethality for a cationic sequence-random copolymer that mimics host-defense antimicrobial peptides. J. Mol. Biol. 379, 38-50; doi:10.1016/j.jmb.2008.03.047
    • (2008) J. Mol. Biol. , vol.379 , pp. 38-50
    • Epand, R.F.1    Mowery, B.P.2    Lee, S.E.3    Stahl, S.S.4    Lehrer, R.I.5    Gellman, S.H.6    Epand, R.M.7
  • 22
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as a predictor of antimicrobial potency
    • doi:10.1021/ja8062327
    • Epand R. M., Rotem S., Mor A., Berno B., Epand R. F. (2008b): Bacterial membranes as a predictor of antimicrobial potency. J. Am. Chem. Soc. 130, 14346-14352; doi:10.1021/ja8062327
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14346-14352
    • Epand, R.M.1    Rotem, S.2    Mor, A.3    Berno, B.4    Epand, R.F.5
  • 23
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • doi:10.1016/j.bbamem.2008.08.023
    • Epand R. M., Epand R. F. (2009): Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochim. Biophys. Acta 1788, 289-294; doi:10.1016/j.bbamem.2008.08.023
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 24
    • 0037436702 scopus 로고    scopus 로고
    • Infectious diseases. Resistant staph finds new niches
    • doi:10.1126/science.299.5613.1639
    • Enserink M. (2003): Infectious diseases. Resistant staph finds new niches. Science 299, 1639-1641; doi:10.1126/science.299.5613.1639
    • (2003) Science , vol.299 , pp. 1639-1641
    • Enserink, M.1
  • 26
    • 0003160911 scopus 로고    scopus 로고
    • Antimicrobial peptides in innate immunity
    • (Ed. K. Lohner), Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • Ganz T., Lehrer R. I. (2001): Antimicrobial peptides in innate immunity. In: Development of Novel Antimicrobial Agents: Emerging Strategies. (Ed. K. Lohner), pp. 139-147, Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 139-147
    • Ganz, T.1    Lehrer, R.I.2
  • 27
    • 0032797883 scopus 로고    scopus 로고
    • An EPR investigation of surfactant action on bacterial membranes
    • doi:10.1111/j.1574-6968.1999.tb13713.x
    • Glover R. E., Smith R. R., Jones M. V., Jackson S. K., Rowlands C. C. (1999): An EPR investigation of surfactant action on bacterial membranes. FEMS Microbiol. Lett. 177, 57-62; doi:10.1111/j.1574-6968.1999.tb13713.x
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 57-62
    • Glover, R.E.1    Smith, R.R.2    Jones, M.V.3    Jackson, S.K.4    Rowlands, C.C.5
  • 28
    • 45749113323 scopus 로고    scopus 로고
    • Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?
    • doi:10.1021/bi800448h
    • Jean-Francois F., Castano S., Desbat B., Odaert B., Roux M., Metz-Boutigue M. H., Dufourc E. J. (2008): Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides? Biochemistry 47, 6394-6402; doi:10.1021/bi800448h
    • (2008) Biochemistry , vol.47 , pp. 6394-6402
    • Jean-Francois, F.1    Castano, S.2    Desbat, B.3    Odaert, B.4    Roux, M.5    Metz-Boutigue, M.H.6    Dufourc, E.J.7
  • 29
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • doi:10.1586/14787210.5.6.951
    • Hale J. D., Hancock R. E. (2007): Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 5, 951-959; doi:10.1586/14787210.5.6.951
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 30
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • doi:10.1111/j.1574-6968.2002.tb11000.x
    • Hancock R. E., Rozek A. (2002): Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206, 143-149; doi:10.1111/j.1574-6968.2002.tb11000.x
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 31
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • DOI 10.1126/science.1129818
    • Hasper H. E., Kramer N. E., Smith J. L., Hillman J. D., Zachariah C., Kuipers O. P., de Kruijff B., Breukink E. (2006): An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313, 1636-1637; doi:10.1126/science.1129818 (Pubitemid 44414037)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6    De Kruijff, B.7    Breukink, E.8
  • 32
    • 40349089737 scopus 로고    scopus 로고
    • Molecular epidemiology of clinically significant antibiotic resistance genes
    • doi:10.1038/sj.bjp.0707632
    • Hawkey P. M. (2008): Molecular epidemiology of clinically significant antibiotic resistance genes. Br. J. Pharmacol. 153, S406-413; doi:10.1038/sj.bjp.0707632
    • (2008) Br. J. Pharmacol. , vol.153
    • Hawkey, P.M.1
  • 33
    • 0034969095 scopus 로고    scopus 로고
    • Factors affecting leakage of trapped solutes from phospholipid vesicles during thermotropic phase transitions
    • DOI 10.1006/cryo.2001.2307
    • Hays L. M., Crowe J. H., Wolkers W., Rudenko S. (2001): Factors affecting leakage of trapped solutes from phospholipid vesicles during thermotropic phase transitions. Cryobiology 42, 88-102; doi:10.1006/cryo.2001.2307 (Pubitemid 32614080)
    • (2001) Cryobiology , vol.42 , Issue.2 , pp. 88-102
    • Hays, L.M.1    Crowe, J.H.2    Wolkers, W.3    Rudenko, S.4
  • 34
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He K., Ludtke S. J., Heller W. T., Huang H. W (1996): Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71, 2669-2679; doi:10.1016/S0006-3495(96)79458-4 (Pubitemid 26367729)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 36
    • 52049111366 scopus 로고    scopus 로고
    • Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases
    • doi:10.1016/j.bbamem.2008.05.014
    • Hickel A., Danner S., Amenitsch H., Degovics G., Rappolt M., Lohner K., Pabst G. (2008): Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases. Biochim. Biophys. Acta 1778, 2325-2333; doi:10.1016/j.bbamem.2008.05.014
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2325-2333
    • Hickel, A.1    Danner, S.2    Amenitsch, H.3    Degovics, G.4    Rappolt, M.5    Lohner, K.6    Pabst, G.7
  • 37
    • 2142695240 scopus 로고    scopus 로고
    • Vancomycin susceptibility within methicillin-resistant Staphylococcus aureus lineages
    • Howe R. A., Monk A., Wootton M., Walsh T. R., Enright M. C. (2004): Vancomycin susceptibility within methicillin-resistant Staphylococcus aureus lineages. Emerg. Infect. Dis. 10, 855-857
    • (2004) Emerg. Infect. Dis. , vol.10 , pp. 855-857
    • Howe, R.A.1    Monk, A.2    Wootton, M.3    Walsh, T.R.4    Enright, M.C.5
  • 38
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • doi:10.1016/j.bbamem.2006.02.001
    • Huang H. W. (2006): Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta 1758, 1292-1302; doi:10.1016/j.bbamem.2006.02.001
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 39
    • 0142240115 scopus 로고    scopus 로고
    • Solubilization of unilamellar egg yolk phosphatidylcholine liposomes by N-alkyl-N,N-dimethylamine N-oxides
    • in Czech
    • Hrubšová A., Karlovská J., Devínsky F., Lacko I., Balgavý P. (2003): Solubilization of unilamellar egg yolk phosphatidylcholine liposomes by N-alkyl-N,N-dimethylamine N-oxides. Ceska Slov. Farm. 52, 299-305 (in Czech)
    • (2003) Ceska Slov. Farm. , vol.52 , pp. 299-305
    • Hrubšová, A.1    Karlovská, J.2    Devínsky, F.3    Lacko, I.4    Balgavý, P.5
  • 40
    • 0019018524 scopus 로고
    • Physical principles of membrane organization
    • doi:10.1017/S0033583500001645
    • Israelachvili J. N., Marcelja S., Horn R. G. (1980): Physical principles of membrane organization. Q. Rev. Biophys. 13, 121-200; doi:10.1017/ S0033583500001645
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 121-200
    • Israelachvili, J.N.1    Marcelja, S.2    Horn, R.G.3
  • 41
    • 1442323941 scopus 로고    scopus 로고
    • Effects of non-ionic surfactants N-alkyl-N,N-dimethylamine-N-oxides on the structure of a phospholipid bilayer: Small-angle X-ray diffraction study
    • doi:10.1016/j.chemphyslip.2003.11.003
    • Karlovská J., Lohner K., Degovics G., Lacko I., Devínsky F., Balgavý P. (2004): Effects of non-ionic surfactants N-alkyl-N,N-dimethylamine-N-oxides on the structure of a phospholipid bilayer: small-angle X-ray diffraction study. Chem. Phys. Lipids 129, 31-41; doi:10.1016/j.chemphyslip.2003.11.003
    • (2004) Chem. Phys. Lipids , vol.129 , pp. 31-41
    • Karlovská, J.1    Lohner, K.2    Degovics, G.3    Lacko, I.4    Devínsky, F.5    Balgavý, P.6
  • 42
    • 0030048521 scopus 로고    scopus 로고
    • Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures
    • doi:10.1016/0005-2736(95)00229-4
    • Keller S. L., Gruner S. M., Gawrisch K. (1996): Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures. Biochim. Biophys. Acta 1278, 241-246; doi:10.1016/0005-2736(95)00229-4
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 241-246
    • Keller, S.L.1    Gruner, S.M.2    Gawrisch, K.3
  • 43
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • doi:10.1016/S0014-5793(03)01154-2
    • Killian J. A. (2003): Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett. 555, 134-138; doi:10.1016/S0014-5793(03)01154-2
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 44
    • 12244268632 scopus 로고    scopus 로고
    • Lipid discrimination in phospholipid monolayers by the antimicrobial frog skin peptide, PGLa. A synchrotron X-ray grazing incidence and reflectivity study
    • doi:10.1007/s00249-002-0233-3
    • Konovalov O., Myagkov I., Struth B., Lohner K. (2002): Lipid discrimination in phospholipid monolayers by the antimicrobial frog skin peptide, PGLa. A synchrotron X-ray grazing incidence and reflectivity study. Eur. Biophys. J. 31, 428-437; doi:10.1007/s00249-002-0233-3
    • (2002) Eur. Biophys. J. , vol.31 , pp. 428-437
    • Konovalov, O.1    Myagkov, I.2    Struth, B.3    Lohner, K.4
  • 45
    • 0031770290 scopus 로고    scopus 로고
    • The mechanism of detergent solubilization of liposomes and protein-containing membranes
    • doi:10.1016/S0006-3495(98)77735-5
    • Kragh-Hansen U., le Maire M., Moller J. V. (1998): The mechanism of detergent solubilization of liposomes and protein-containing membranes. Biophys. J. 75, 2932-2946; doi:10.1016/S0006-3495(98)77735-5
    • (1998) Biophys. J. , vol.75 , pp. 2932-2946
    • Kragh-Hansen, U.1    Le Maire, M.2    Moller, J.V.3
  • 47
    • 0030863833 scopus 로고    scopus 로고
    • Structural aspects of the interaction of peptidyl-glycyl-leucine- carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids
    • doi:10.1111/j.1432-1033.1997.00938.x
    • Latal A., Degovics G., Epand R. F., Epand R. M., Lohner K. (1997): Structural aspects of the interaction of peptidyl-glycyl-leucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. Eur. J. Biochem. 248, 938-946; doi:10.1111/j.1432-1033.1997.00938.x
    • (1997) Eur. J. Biochem. , vol.248 , pp. 938-946
    • Latal, A.1    Degovics, G.2    Epand, R.F.3    Epand, R.M.4    Lohner, K.5
  • 48
    • 33751222275 scopus 로고    scopus 로고
    • Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity
    • DOI 10.1529/biophysj.106.090118
    • Li C., Salditt T. (2006): Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity. Biophys. J. 91, 3285-3300; doi:10.1529/biophysj.106.090118 (Pubitemid 44788263)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3285-3300
    • Li, C.1    Salditt, T.2
  • 49
    • 0026084947 scopus 로고
    • Effects of small organic molecules on phospholipid phase transitions
    • doi:10.1016/0009-3084(91)90085-P
    • Lohner K. (1991): Effects of small organic molecules on phospholipid phase transitions. Chem. Phys. Lipids 57, 341-362; doi:10.1016/0009-3084(91) 90085-P
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 341-362
    • Lohner, K.1
  • 50
    • 0027376103 scopus 로고
    • Squalene promotes the formation of non-bilayer structures in phospholipid model membranes
    • doi:10.1016/0005-2736(93)90232-90240
    • Lohner K., Degovics G., Laggner P., Gnamusch E., Paltauf F. (1993): Squalene promotes the formation of non-bilayer structures in phospholipid model membranes. Biochim. Biophys. Acta 1152, 69-77; doi:10.1016/0005-2736(93)90232- 90240
    • (1993) Biochim. Biophys. Acta , vol.1152 , pp. 69-77
    • Lohner, K.1    Degovics, G.2    Laggner, P.3    Gnamusch, E.4    Paltauf, F.5
  • 51
    • 0030586129 scopus 로고    scopus 로고
    • Is the high propensity of ethanolamine plasmalogens to form non-lamellar lipid structures manifested in the properties of biomembranes?
    • doi:10.1016/0009-3084(96)02580-7
    • Lohner K. (1996): Is the high propensity of ethanolamine plasmalogens to form non-lamellar lipid structures manifested in the properties of biomembranes? Chem. Phys. Lipids 81, 167-184; doi:10.1016/0009-3084(96)02580-7
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 167-184
    • Lohner, K.1
  • 52
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • DOI 10.1021/bi961300p
    • Lohner K., Latal A., Lehrer R. I., Ganz T. (1997): Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems. Biochemistry 36, 1525-1531; doi:10.1021/bi961300p (Pubitemid 27074977)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 53
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • doi:10.1016/S0005-2736(99)00204-7
    • Lohner K., Prenner E. J. (1999): Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim. Biophys. Acta 1462, 141-156; doi:10.1016/S0005-2736(99)00204-7
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 55
    • 0002336563 scopus 로고    scopus 로고
    • The role of membrane lipid composition in cell targeting of antimicrobial peptides
    • Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • Lohner K. (2001b): The role of membrane lipid composition in cell targeting of antimicrobial peptides. In: Development of Novel Antimicrobial Agents: Emerging Strategies, pp. 149-165, Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1
  • 56
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics
    • doi:10.2174/1386207053764576
    • Lohner K., Blondelle S. E. (2005): Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics. Comb. Chem. High Throughput Screen. 8, 239-255; doi:10.2174/1386207053764576
    • (2005) Comb. Chem. High Throughput Screen. , vol.8 , pp. 239-255
    • Lohner, K.1    Blondelle, S.E.2
  • 57
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • doi:10.1021/bi00051a026
    • Ludtke S., He K., Huang H. W. (1995): Membrane thinning caused by magainin 2. Biochemistry 34, 16764-16769doi:10.1021/bi00051a026
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.W.3
  • 58
    • 0029904095 scopus 로고    scopus 로고
    • Membrane pores induced by magainin
    • DOI 10.1021/bi9620621
    • Ludtke S. J., He K., Heller W. T., Harroun T. A., Yang L., Huang H. W. (1996): Membrane pores induced by magainin. Biochemistry 35, 13723-13728; doi:10.1021/bi9620621 (Pubitemid 26363914)
    • (1996) Biochemistry , vol.35 , Issue.43 , pp. 13723-13728
    • Ludtke, S.J.1    He, K.2    Heller, W.T.3    Harroun, T.A.4    Yang, L.5    Huang, H.W.6
  • 59
    • 33747038638 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes
    • doi:10.1111/j.1365-2958.2006.05317.x
    • Matsumoto K., Kusaka J., Nishibori A., Hara H. (2006): Lipid domains in bacterial membranes. Mol. Microbiol. 61, 1110-1117; doi:10.1111/j.1365-2958. 2006.05317.x
    • (2006) Mol. Microbiol. , vol.61 , pp. 1110-1117
    • Matsumoto, K.1    Kusaka, J.2    Nishibori, A.3    Hara, H.4
  • 60
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • doi:10.1021/bi00039a009
    • Matsuzaki K., Murase O., Miyajima K. (1995): Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 34, 12553-12559; doi:10.1021/bi00039a009
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 61
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • DOI 10.1021/bi960016v
    • Matsuzaki K., Murase O., Fujii N., Miyajima K. (1996): An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368; doi:10.1021/bi960016v (Pubitemid 26299310)
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 62
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • doi:10.1016/S0005-2736(97)00051-55
    • Matsuzaki K., Sugishita K., Harada M., Fujii N., Miyajima K. (1997): Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327, 119-130; doi:10.1016/S0005-2736(97)00051-55
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 63
    • 0032566283 scopus 로고    scopus 로고
    • Relationship of membrane curvature to the formation of pores by magainin 2
    • doi:10.1021/bi980539y
    • Matsuzaki K., Sugishita K., Ishibe N., Ueha M., Nakata S., Miyajima K., Epand R. M. (1998): Relationship of membrane curvature to the formation of pores by magainin 2. Biochemistry 37, 11856-11863; doi:10.1021/bi980539y
    • (1998) Biochemistry , vol.37 , pp. 11856-11863
    • Matsuzaki, K.1    Sugishita, K.2    Ishibe, N.3    Ueha, M.4    Nakata, S.5    Miyajima, K.6    Epand, R.M.7
  • 64
    • 0003401938 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides
    • (Ed. K. Lohner), Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • Matsuzaki K. (2001): Molecular mechanisms of membrane perturbation by antimicrobial peptides. In: Development of Novel Antimicrobial Agents: Emerging Strategies. (Ed. K. Lohner), pp. 167-181, Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 167-181
    • Matsuzaki, K.1
  • 65
    • 0001223593 scopus 로고
    • Membrane structure
    • (Eds. J. Maniloff, R. N. McElhaney, L. R. Finch and J. B. Baseman), American Society for Microbiology, Washington DC
    • McElhaney R. N. (1992): Membrane structure. In: Mycoplasmas: Molecular Biology and Pathogenesis. (Eds. J. Maniloff, R. N. McElhaney, L. R. Finch and J. B. Baseman), pp. 113-155, American Society for Microbiology, Washington DC
    • (1992) Mycoplasmas: Molecular Biology and Pathogenesis , pp. 113-155
    • McElhaney, R.N.1
  • 66
    • 15744398051 scopus 로고    scopus 로고
    • Role of membrane lipids in bacterial division-site selection
    • doi:10.1016/j.mib.2005.02.012
    • Mileykovskaya E., Dowhan W. (2005): Role of membrane lipids in bacterial division-site selection. Curr. Opin. Microbiol. 8, 135-142; doi:10.1016/j.mib. 2005.02.012
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 135-142
    • Mileykovskaya, E.1    Dowhan, W.2
  • 67
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • DOI 10.1128/JB.182.4.1172-1175.2000
    • Mileykovskaya E., Dowhan W. (2000): Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182, 1172-1175; doi:10.1128/JB.182.4. 1172-1175.2000 (Pubitemid 30075045)
    • (2000) Journal of Bacteriology , vol.182 , Issue.4 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 68
    • 0031856847 scopus 로고    scopus 로고
    • Localization and function of early cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine
    • Mileykovskaya E., Sun Q., Margolin W., Dowhan W. (1998): Localization and function of early cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine. J. Bacteriol. 180, 4252-4257 (Pubitemid 28373532)
    • (1998) Journal of Bacteriology , vol.180 , Issue.16 , pp. 4252-4257
    • Mileykovskaya, E.1    Sun, Q.2    Margolin, W.3    Dowhan, W.4
  • 69
    • 0029975929 scopus 로고    scopus 로고
    • Wildtype Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures
    • doi:10.1074/jbc.271.12.6801
    • Morein S., Andersson A., Rilfors L., Lindblom G. (1996): Wildtype Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures. J. Biol. Chem. 271, 6801-6809; doi:10.1074/jbc.271.12.6801
    • (1996) J. Biol. Chem. , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.2    Rilfors, L.3    Lindblom, G.4
  • 70
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S., Niwa M., Takao T., Shimonishi Y. (1988): Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem. 263, 16709-16713
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 72
    • 0035118091 scopus 로고    scopus 로고
    • Hypothesis: Membrane domains and hyperstructures control bacterial division
    • DOI 10.1016/S0300-9084(00)01203-7
    • Norris V., Fishov I. (2001): Hypothesis: membrane domains and hyperstructures control bacterial division. Biochimie 83, 91-97; doi:10.1016/S0300-9084(00)01203-7 (Pubitemid 32181529)
    • (2001) Biochimie , vol.83 , Issue.1 , pp. 91-97
    • Norris, V.1    Fishov, I.2
  • 73
    • 2142768752 scopus 로고    scopus 로고
    • Molecular mechanism of cell selectivity by linear amphipatic α-helical and diasteriomeric antimicrobial peptides
    • (Ed. K. Lohner), Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • Oren Z., Shai Y. (2001): Molecular mechanism of cell selectivity by linear amphipatic α-helical and diasteriomeric antimicrobial peptides. In: Development of Novel Antimicrobial Agents: Emerging Strategies. (Ed. K. Lohner), pp. 183-204, Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 183-204
    • Oren, Z.1    Shai, Y.2
  • 74
    • 36248957675 scopus 로고    scopus 로고
    • Entropy-driven softening of fluid lipid bilayers by alamethicin
    • DOI 10.1021/la701586c
    • Pabst G., Danner S., Podgornik R., Katsaras J. (2007): Entropy-driven softening of fluid lipid bilayers by alamethicin. Langmuir 23, 11705-11711; doi:10.1021/la701586c (Pubitemid 350133018)
    • (2007) Langmuir , vol.23 , Issue.23 , pp. 11705-11711
    • Pabst, G.1    Danner, S.2    Podgornik, R.3    Katsaras, J.4
  • 76
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • doi:10.1016/j.peptides.2003.08.023
    • Powers J. P. S., Hancock R. E. W. (2003): The relationship between peptide structure and antibacterial activity. Peptides 24, 1681-1691; doi:10.1016/j.peptides.2003.08.023
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.S.1    Hancock, R.E.W.2
  • 77
    • 0038298731 scopus 로고    scopus 로고
    • Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction
    • Rappolt M., Hickel A., Bringezu F., Lohner K. (2003): Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction. Biophys. J. 84, 3111-3122; doi:10.1016/S0006-3495(03)70036-8 (Pubitemid 36531759)
    • (2003) Biophysical Journal , vol.84 , Issue.5 , pp. 3111-3122
    • Rappolt, M.1    Hickel, A.2    Bringezu, F.3    Lohner, K.4
  • 78
    • 0028785891 scopus 로고
    • Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli
    • Rietveld A. G., Koorengevel M. C., de Kruijff B. (1995): Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J. 14, 5506-5513
    • (1995) EMBO J. , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 79
    • 0027346050 scopus 로고
    • Mycoplasma cell membranes
    • (Ed. S. Rottem and I. Kahane), Plenum Press, New York
    • Rilfors L., Wieslander A., Lindblom G. (1993): Mycoplasma cell membranes. In: Subcellular Biochemistry. (Ed. S. Rottem and I. Kahane), Vol.20, pp. 109-166, Plenum Press, New York
    • (1993) Subcellular Biochemistry , vol.20 , pp. 109-166
    • Rilfors, L.1    Wieslander, A.2    Lindblom, G.3
  • 80
    • 0017356323 scopus 로고
    • Membrane asymmetry
    • doi:10.1126/science.402030
    • Rothman J. E., Leonard J. (1977): Membrane asymmetry. Science 195, 743-753; doi:10.1126/science.402030
    • (1977) Science , vol.195 , pp. 743-753
    • Rothman, J.E.1    Leonard, J.2
  • 81
    • 33845549925 scopus 로고
    • Lipid chain length and temperature dependence of ethanol- phosphatidylcholine interactions
    • doi:10.1021/bi00283a001
    • Rowe E. S. (1983): Lipid chain length and temperature dependence of ethanol-phosphatidylcholine interactions. Biochemistry 22, 3299-3305; doi:10.1021/bi00283a001
    • (1983) Biochemistry , vol.22 , pp. 3299-3305
    • Rowe, E.S.1
  • 83
    • 34948829603 scopus 로고    scopus 로고
    • How lipids influence the mode of action of membrane-active peptides
    • doi:10.1016/j.bbamem.2007.06.015
    • Sevcsik E., Pabst G., Jilek A., Lohner K. (2007): How lipids influence the mode of action of membrane-active peptides. Biochim. Biophys. Acta 1768, 2586-2595; doi:10.1016/j.bbamem.2007.06.015
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2586-2595
    • Sevcsik, E.1    Pabst, G.2    Jilek, A.3    Lohner, K.4
  • 84
    • 45849085763 scopus 로고    scopus 로고
    • Interaction of LL-37 with model membrane systems of different complexity: Influence of the lipid matrix
    • doi:10.1529/biophysj.107.123620
    • Sevcsik E., Pabst G., Richter W., Danner S., Amenitsch H., Lohner K. (2008): Interaction of LL-37 with model membrane systems of different complexity: influence of the lipid matrix. Biophys J. 94, 4688-4699; doi:10.1529/biophysj.107.123620
    • (2008) Biophys J. , vol.94 , pp. 4688-4699
    • Sevcsik, E.1    Pabst, G.2    Richter, W.3    Danner, S.4    Amenitsch, H.5    Lohner, K.6
  • 85
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • doi:10.1002/bip.10260
    • Shai Y. (2002): Mode of action of membrane active antimicrobial peptides. Biopolymers 66, 236-248; doi:10.1002/bip.10260
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 86
    • 0025311581 scopus 로고
    • Lamellar/inverted cubic (Lα/QII) phase transition in N-methylateddioleoylphosphatidylethanolamine
    • doi:10.1021/bi00477a014
    • Siegel D. P., Banschbach J. L. (1990): Lamellar/inverted cubic (Lα/QII) phase transition in N-methylateddioleoylphosphatidylethanolamine. Biochemistry 29, 5975-5981; doi:10.1021/bi00477a014
    • (1990) Biochemistry , vol.29 , pp. 5975-5981
    • Siegel, D.P.1    Banschbach, J.L.2
  • 87
    • 0021761592 scopus 로고
    • Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions
    • doi:10.1016/0005-2736(84)90562-5
    • Simon S. A., McIntosh T. J. (1984): Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions. Biochim. Biophys. Acta 773, 169-172; doi:10.1016/0005-2736(84)90562-5
    • (1984) Biochim. Biophys. Acta , vol.773 , pp. 169-172
    • Simon, S.A.1    McIntosh, T.J.2
  • 88
    • 0036195459 scopus 로고    scopus 로고
    • Antimicrobial resistance: A global response
    • WHO
    • Smith R. D., Coast J. (2002): Antimicrobial resistance: a global response. Bull. WHO 80, 126-133
    • (2002) Bull , vol.80 , pp. 126-133
    • Smith, R.D.1    Coast, J.2
  • 89
    • 0034730576 scopus 로고    scopus 로고
    • X-ray studies on the interaction of gramicidin S with microbial lipid extracts: Evidence for cubic phase formation
    • doi:10.1016/S0005-2736(00)00260-261
    • Staudegger E., Prenner E. J., Kriechbaum M., Degovics G., Lewis R. N. A. H., McElhaney R. N., Lohner K. (2000): X-ray studies on the interaction of gramicidin S with microbial lipid extracts: evidence for cubic phase formation. Biochim. Biophys. Acta 1468, 213-230; doi:10.1016/S0005-2736(00)00260-261
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 213-230
    • Staudegger, E.1    Prenner, E.J.2    Kriechbaum, M.3    Degovics, G.4    Lewis, R.N.A.H.5    McElhaney, R.N.6    Lohner, K.7
  • 90
    • 33646135796 scopus 로고    scopus 로고
    • Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: Structural fidelity of 2H-labels versus high sensitivity of 19F-NMR
    • doi:10.1529/biophysj.105.073858
    • Strandberg E., Wadhwani P., Tremouilhac P., Durr U. H., Ulrich A. S. (2006): Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR. Biophys. J. 90, 1676-1686; doi:10.1529/biophysj.105.073858
    • (2006) Biophys. J. , vol.90 , pp. 1676-1686
    • Strandberg, E.1    Wadhwani, P.2    Tremouilhac, P.3    Durr, U.H.4    Ulrich, A.S.5
  • 91
    • 0142172772 scopus 로고    scopus 로고
    • Small-angle neutron scattering study of N-dodecyl-N,N-dimethylamine N-oxide induced solubilization of dioleoylphosphatidylcholine bilayers in liposomes
    • Uhríková D., Kučerka N., Islamov A., Gordeliy V., Balgavý P. (2001): Small-angle neutron scattering study of N-dodecyl-N,N-dimethylamine N-oxide induced solubilization of dioleoylphosphatidylcholine bilayers in liposomes. Gen. Physiol. Biophys. 20, 183-189
    • (2001) Gen. Physiol. Biophys. , vol.20 , pp. 183-189
    • Uhríková, D.1    Kučerka, N.2    Islamov, A.3    Gordeliy, V.4    Balgavý, P.5
  • 92
    • 0042565977 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids
    • doi:10.1046/j.1365-2958.2003.03614.x
    • Vanounou S., Parola A. H., Fishov I. (2003): Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids. Mol. Microbiol. 49, 1067-1079; doi:10.1046/j.1365-2958.2003.03614.x
    • (2003) Mol. Microbiol. , vol.49 , pp. 1067-1079
    • Vanounou, S.1    Parola, A.H.2    Fishov, I.3
  • 93
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensin
    • doi:10.1016/0959-440X(95)80038-7
    • White S. H., Wimley W. C., Selsted M. E. (1995): Structure, function, and membrane integration of defensin. Curr. Opin. Struct. Biol. 5, 521-527; doi:10.1016/0959-440X(95)80038-7
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 94
    • 0029022547 scopus 로고
    • X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: Diphytanoyl phosphatidylcholine with alamethicin at low concentrations
    • doi:10.1016/S0006-3495(95)80418-2
    • Wu Y., He K., Ludtke S. J., Huang H. W. (1995): X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentrations. Biophys. J. 68, 2361-2369; doi:10.1016/S0006-3495(95)80418-2
    • (1995) Biophys. J. , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 95
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • doi:10.1016/S0006-3495(01)
    • Yang L., Harroun T. A., Weiss T. M., Ding L., Huang H. W. (2001): Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81, 1475-1485; doi:10.1016/S0006-3495(01)
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 96
    • 0002017229 scopus 로고
    • Biological distribution
    • (Ed. G. Cevc), Marcel Dekker, Inc., New York
    • Yorek M. A. (1993): Biological distribution. In: Phospholipids Handbook. (Ed. G. Cevc), pp. 745-775, Marcel Dekker, Inc., New York
    • (1993) Phospholipids Handbook , pp. 745-775
    • Yorek, M.A.1
  • 97
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • doi:10.1038/415389a
    • Zasloff M. (2002): Antimicrobial peptides of multicellular organisms. Nature 415, 389-395; doi:10.1038/415389a
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 98
    • 40849102416 scopus 로고    scopus 로고
    • Membrane curvature stress and antibacterial activity of lactoferricin derivatives
    • doi:10.1016/j.bbrc.2008.01.176
    • Zweytick D., Tumer S., Blondelle S. E., Lohner K. (2008): Membrane curvature stress and antibacterial activity of lactoferricin derivatives. Biochem. Biophys. Res. Commun. 369, 395-400; doi:10.1016/j.bbrc.2008.01.176
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 395-400
    • Zweytick, D.1    Tumer, S.2    Blondelle, S.E.3    Lohner, K.4


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