메뉴 건너뛰기




Volumn 51, Issue 2, 2012, Pages 149-177

Role of lipids in the interaction of antimicrobial peptides with membranes

Author keywords

Antimicrobial peptide; Cell death; Immunity; Intracellular targets; Mechanism of action; Membrane permeabilization; Membrane topology; Peptide design; Phospholipids; Resistance; Structure activity relationship; Target activity; Therapeutic agents

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIOCIN; BUFORIN II; DEFENSIN; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE IV; DPK 060; INDOLICIDIN; ISEGANAN; LACTOFERRICIN; LACTOFERRIN; LACTOFERRIN[1-11]; LIPID; MELITTIN; MX 594AN; NISIN; OMIGANAN; OPEBACAN; PEPTIDOGLYCAN RECOGNITION PROTEIN; PERGAMUM; PLACEBO; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; QUINOLINE DERIVED ANTIINFECTIVE AGENT; SULFONAMIDE; TRIMETHOPRIM; UNCLASSIFIED DRUG;

EID: 84856774559     PISSN: 01637827     EISSN: 18732194     Source Type: Journal    
DOI: 10.1016/j.plipres.2011.12.005     Document Type: Review
Times cited : (571)

References (280)
  • 1
    • 13844315653 scopus 로고    scopus 로고
    • A re-evaluation of the role of host defence peptides in mammalian immunity
    • DOI 10.2174/1389203053027494
    • D.M.E. Bowdish, D.J. Davidson, and R.E.W.H. Hancock A re-evaluation of the role of host defence peptides in mammalian immunity Curr Protein Pept Sci 6 2005 35 51 (Pubitemid 40259800)
    • (2005) Current Protein and Peptide Science , vol.6 , Issue.1 , pp. 35-51
    • Bowdish, D.M.E.1    Davidson, D.J.2    Hancock, R.E.W.3
  • 2
    • 69249096200 scopus 로고    scopus 로고
    • The roles of antimicrobial peptides in innate host defense
    • G. Diamond, N. Beckloff, A. Weinberg, and K.O. Kisich The roles of antimicrobial peptides in innate host defense Curr Pharm Des 15 2009 2377 2392
    • (2009) Curr Pharm des , vol.15 , pp. 2377-2392
    • Diamond, G.1    Beckloff, N.2    Weinberg, A.3    Kisich, K.O.4
  • 3
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • R. Hancock, and G. Diamond The role of cationic antimicrobial peptides in innate host defences Trends Microbiol 8 2000 402 410
    • (2000) Trends Microbiol , vol.8 , pp. 402-410
    • Hancock, R.1    Diamond, G.2
  • 4
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • DOI 10.1021/bi000946l
    • H.W. Huang Action of antimicrobial peptides: two-state model Biochemistry 39 2000 8347 8352 (Pubitemid 30489931)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 6
    • 35448929949 scopus 로고    scopus 로고
    • Analysis and prediction of antibacterial peptides
    • S. Lata, B. Sharma, and G. Raghava Analysis and prediction of antibacterial peptides BMC Bioinformatics 8 2007 263
    • (2007) BMC Bioinformatics , vol.8 , pp. 263
    • Lata, S.1    Sharma, B.2    Raghava, G.3
  • 7
    • 75649127958 scopus 로고    scopus 로고
    • Antibacterial activity and synergism of the hybrid antimicrobial peptide, CAMA-syn
    • K.-W. Jeong, S. Shin, J.-K. Kim, and Y. Kim Antibacterial activity and synergism of the hybrid antimicrobial peptide, CAMA-syn Bull Korean Chem Soc 30 2009 1839 1844
    • (2009) Bull Korean Chem Soc , vol.30 , pp. 1839-1844
    • Jeong, K.-W.1    Shin, S.2    Kim, J.-K.3    Kim, Y.4
  • 10
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • DOI 10.1074/jbc.M507042200
    • E. Glukhov, M. Stark, L.L. Burrows, and C.M. Deber Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes J Biol Chem 280 2005 33960 33967 (Pubitemid 41443116)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 11
    • 1042267410 scopus 로고    scopus 로고
    • Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?
    • DOI 10.1016/j.peptides.2003.09.013
    • N. Papo, and Y. Shai Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes? Peptides 24 2003 1693 1703 (Pubitemid 38198076)
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 12
    • 43649090328 scopus 로고    scopus 로고
    • Cholesterol, lanosterol, and ergosterol attenuate the membrane association of LL-37(W27F) and temporin L
    • R. Sood, and P.K.J. Kinnunen Cholesterol, lanosterol, and ergosterol attenuate the membrane association of LL-37(W27F) and temporin L Biochim Biophys Acta (BBA) - Biomembr 1778 2008 1460 1466
    • (2008) Biochim Biophys Acta (BBA) - Biomembr , vol.1778 , pp. 1460-1466
    • Sood, R.1    Kinnunen, P.K.J.2
  • 13
    • 0034767060 scopus 로고    scopus 로고
    • Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin
    • H. Zhao, J.-P. Mattila, J.M. Holopainen, and P.K.J. Kinnunen Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin Biophys J 81 2001 2979 2991 (Pubitemid 33020082)
    • (2001) Biophysical Journal , vol.81 , Issue.5 , pp. 2979-2991
    • Zhao, H.1    Mattila, J.-P.2    Holopainen, J.M.3    Kinnunen, P.K.J.4
  • 14
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic [alpha]-helical cationic antimicrobial peptides
    • Z. Jiang, A.I. Vasil, J.D. Hale, R.E.W. Hancock, M.L. Vasil, and R.S. Hodges Effects of net charge and the number of positively charged residues on the biological activity of amphipathic [alpha]-helical cationic antimicrobial peptides Pept Sci 90 2008 369 383
    • (2008) Pept Sci , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 16
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • DOI 10.1016/j.coi.2005.11.004, PII S0952791505001998, Innate Immunity/Antigen Processing and Recognition
    • K.L. Brown, and R.E.W. Hancock Cationic host defense (antimicrobial) peptides Curr Opin Immunol 18 2006 24 30 (Pubitemid 43049644)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 17
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • DOI 10.1002/bip.10260
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248 (Pubitemid 36098316)
    • (2002) Biopolymers - Peptide Science Section , vol.66 , Issue.4 , pp. 236-248
    • Shai, Y.1
  • 19
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 21
    • 55449131941 scopus 로고    scopus 로고
    • The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm
    • A.B. Mochon, and H. Liu The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm PLoS Pathog 4 2008 1 12
    • (2008) PLoS Pathog , vol.4 , pp. 1-12
    • Mochon, A.B.1    Liu, H.2
  • 22
    • 55549117806 scopus 로고    scopus 로고
    • Histatins are the major wound-closure stimulating factors in human saliva as identified in a cell culture assay
    • M.J. Oudhoff, J.G.M. Bolscher, K. Nazmi, H. Kalay, W. Van 't Hof, and A.V.N. Amerongen Histatins are the major wound-closure stimulating factors in human saliva as identified in a cell culture assay FASEB J 22 2008 3805 3812
    • (2008) FASEB J , vol.22 , pp. 3805-3812
    • Oudhoff, M.J.1    Bolscher, J.G.M.2    Nazmi, K.3    Kalay, H.4    Van 'T Hof, W.5    Amerongen, A.V.N.6
  • 23
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • W.F. Broekaert, F. Terras, B. Cammue, and R.W. Osborn Plant defensins: novel antimicrobial peptides as components of the host defense system Plant Physiol 108 1995 1353 1358
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.2    Cammue, B.3    Osborn, R.W.4
  • 25
    • 33749376461 scopus 로고    scopus 로고
    • A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer
    • DOI 10.1074/jbc.M606031200
    • Y. Rosenfeld, D. Barra, M. Simmaco, Y. Shai, and M.L. Mangoni A synergism between temporins toward gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer J Biol Chem 281 2006 28565 28574 (Pubitemid 44506999)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28565-28574
    • Rosenfeld, Y.1    Barra, D.2    Simmaco, M.3    Shai, Y.4    Mangoni, M.L.5
  • 26
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • M.N. Melo, R. Ferre, and M.A.R.B. Castanho Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations Nat Rev Microbiol 7 2009 245 250
    • (2009) Nat Rev Microbiol , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • DOI 10.1124/pr.55.1.2
    • M.R. Yeaman, and N.Y. Yount Mechanisms of antimicrobial peptide action and resistance Pharmacol Rev 55 2003 27 55 (Pubitemid 36268398)
    • (2003) Pharmacological Reviews , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
    • 0033003473 scopus 로고    scopus 로고
    • Biological properties of structurally related α-helical cationic antimicrobial peptides
    • M.G. Scott, H. Yan, and R.E.W. Hancock Biological properties of structurally related [alpha]-helical cationic antimicrobial peptides Infect Immun 67 1999 2005 2009 (Pubitemid 29144428)
    • (1999) Infection and Immunity , vol.67 , Issue.4 , pp. 2005-2009
    • Scott, M.G.1    Yan, H.2    Hancock, R.E.W.3
  • 29
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • DOI 10.1007/s00018-007-6475-6
    • N. Mookherjee, and R. Hancock Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections Cell Mol Life Sci 64 2007 922 933 (Pubitemid 46597762)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.7-8 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.W.2
  • 30
    • 85047685350 scopus 로고    scopus 로고
    • Using antimicrobial host defense peptides as anti-infective and immunomodulatory agents
    • T. Kruse, and H.-H. Kristensen Using antimicrobial host defense peptides as anti-infective and immunomodulatory agents Expert Rev Anti Infect Ther 6 2008 887 895
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 887-895
    • Kruse, T.1    Kristensen, H.-H.2
  • 31
    • 79952583993 scopus 로고    scopus 로고
    • Human anti-microbial cathelicidin peptide LL-37 suppresses the LPS-induced apoptosis of endothelial cells
    • K. Suzuki, T. Murakami, K. Kuwahara-Arai, H. Tamura, K. Hiramatsu, and I. Nagaoka Human anti-microbial cathelicidin peptide LL-37 suppresses the LPS-induced apoptosis of endothelial cells Int Immunol 23 2011 185 193
    • (2011) Int Immunol , vol.23 , pp. 185-193
    • Suzuki, K.1    Murakami, T.2    Kuwahara-Arai, K.3    Tamura, H.4    Hiramatsu, K.5    Nagaoka, I.6
  • 34
    • 0029824838 scopus 로고    scopus 로고
    • Antiendotoxin activity of cationic peptide antimicrobial agents
    • M. Gough, R. Hancock, and N. Kelly Antiendotoxin activity of cationic peptide antimicrobial agents Infect Immun 64 1996 4922 4927 (Pubitemid 26403942)
    • (1996) Infection and Immunity , vol.64 , Issue.12 , pp. 4922-4927
    • Gough, M.1    Hancock, R.E.W.2    Kelly, N.M.3
  • 35
    • 0029460562 scopus 로고
    • Structure and functions of endotoxin-binding peptides derived from CAP18
    • M. Hirata, J. Zhong, S.C. Wright, and J.W. Larrick Structure and functions of endotoxin-binding peptides derived from CAP18 Prog Clin Biol Res 392 1995 317 326
    • (1995) Prog Clin Biol Res , vol.392 , pp. 317-326
    • Hirata, M.1    Zhong, J.2    Wright, S.C.3    Larrick, J.W.4
  • 36
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • DOI 10.1016/S0022-1759(99)00152-0, PII S0022175999001520
    • G.H. Gudmundsson, and B. Agerberth Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system J Immunol Methods 232 1999 45 54 (Pubitemid 30017764)
    • (1999) Journal of Immunological Methods , vol.232 , Issue.1-2 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 39
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • DOI 10.1016/S1471-4906(02)02246-9, PII S1471490602022469
    • D. Yang, A. Biragyn, L.W. Kwak, and J.J. Oppenheim Mammalian defensins in immunity: more than just microbicidal Trends Immunol 23 2002 291 296 (Pubitemid 34628771)
    • (2002) Trends in Immunology , vol.23 , Issue.6 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 40
    • 69949086979 scopus 로고    scopus 로고
    • Potential of immunomodulatory host defense peptides as novel anti-infectives
    • D.M. Easton, A. Nijnik, M.L. Mayer, and R.E.W. Hancock Potential of immunomodulatory host defense peptides as novel anti-infectives Trends Biotechnol 27 2009 582 590
    • (2009) Trends Biotechnol , vol.27 , pp. 582-590
    • Easton, D.M.1    Nijnik, A.2    Mayer, M.L.3    Hancock, R.E.W.4
  • 41
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, [alpha]-helical antimicrobial peptides
    • A. Tossi, L. Sandri, and A. Giangaspero Amphipathic, [alpha]-helical antimicrobial peptides Biopolymers 55 2000 4 30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 42
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic [alpha]-helical antimicrobial peptides
    • A. Giangaspero, L. Sandri, and A. Tossi Amphipathic [alpha]-helical antimicrobial peptides Eur J Biochem 268 2001 5589 5600
    • (2001) Eur J Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 44
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: Obstacles and realistic outlook
    • DOI 10.1016/j.coph.2006.04.006, PII S1471489206001299, Anti-infectives/New Technologies
    • A.K. Marr, W.J. Gooderham, and R.E.W. Hancock Antibacterial peptides for therapeutic use: obstacles and realistic outlook Curr Opin Pharmacol 6 2006 468 472 (Pubitemid 44340665)
    • (2006) Current Opinion in Pharmacology , vol.6 , Issue.5 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3
  • 45
    • 79953148897 scopus 로고    scopus 로고
    • Alpha-helical cationic antimicrobial peptides: Relationships of structure and function
    • Y. Huang, J. Huang, and Y. Chen Alpha-helical cationic antimicrobial peptides: relationships of structure and function Protein Cell 1 2010 143 152
    • (2010) Protein Cell , vol.1 , pp. 143-152
    • Huang, Y.1    Huang, J.2    Chen, Y.3
  • 46
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim Biophys Acta (BBA) - Biomembr 1462 1999 11 28
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 47
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides: The ancient arm of the human immune system
    • J. Wiesner, and A. Vilcinskas antimicrobial peptides: the ancient arm of the human immune system Virulence 1 2010 440 464
    • (2010) Virulence , vol.1 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2
  • 48
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 49
    • 70349117723 scopus 로고    scopus 로고
    • Amphipathic β-Strand mimics as potential membrane disruptive antibiotics
    • J.L. Watson, and E.R. Gillies Amphipathic β-Strand mimics as potential membrane disruptive antibiotics J Org Chem 74 2009 5953 5960
    • (2009) J Org Chem , vol.74 , pp. 5953-5960
    • Watson, J.L.1    Gillies, E.R.2
  • 50
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim Biophys Acta (BBA) - Biomembr 1462 1999 1 10
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 52
    • 0041322755 scopus 로고    scopus 로고
    • Helical structure of dermaseptin B2 in a membrane-mimetic environment
    • DOI 10.1021/bi034401d
    • O. Lequin, F. Bruston, O. Convert, G. Chassaing, and P. Nicolas Helical structure of dermaseptin B2 in a membrane-mimetic environment Biochemistry 42 2003 10311 10323 (Pubitemid 37052053)
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10311-10323
    • Lequin, O.1    Bruston, F.2    Convert, O.3    Chassaing, G.4    Nicolas, P.5
  • 53
    • 0942279702 scopus 로고    scopus 로고
    • Investigating the Importance of the Flexible Hinge in Caerin 1.1: Solution Structures and Activity of Two Synthetically Modified Caerin Peptides
    • T.L. Pukala, C.S. Brinkworth, J.A. Carver, and J.H. Bowie Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides Biochemistry 43 2004 937 944 (Pubitemid 38141491)
    • (2004) Biochemistry , vol.43 , Issue.4 , pp. 937-944
    • Pukala, T.L.1    Brinkworth, C.S.2    Carver, J.A.3    Bowie, J.H.4
  • 55
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: A nuclear magnetic resonance and dynamical simulated annealing study
    • T.A. Holak, A. Engstroem, P.J. Kraulis, G. Lindeberg, H. Bennich, and T.A. Jones The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study Biochemistry 27 1988 7620 7629
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engstroem, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6
  • 56
    • 0033863799 scopus 로고    scopus 로고
    • Membrane-induced folding of cecropin A
    • L. Silvestro, and P.H. Axelsen Membrane-induced folding of cecropin A Biophys J 79 2000 1465 1477
    • (2000) Biophys J , vol.79 , pp. 1465-1477
    • Silvestro, L.1    Axelsen, P.H.2
  • 57
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • DOI 10.1007/s002329900201
    • B. Bechinger Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin J Membr Biol 156 1997 197 211 (Pubitemid 27208423)
    • (1997) Journal of Membrane Biology , vol.156 , Issue.3 , pp. 197-211
    • Bechinger, B.1
  • 59
    • 0025280240 scopus 로고
    • Raman spectroscopy of synthetic antimicrobial frog peptides magainin 2a and PGLa
    • DOI 10.1021/bi00470a031
    • R.W. Williams, R. Starman, K.M.P. Taylor, K. Gable, T. Beeler, and M. Zasloff Raman spectroscopy of synthetic antimicrobial frog peptides magainin 2a and PGLa Biochemistry 29 1990 4490 4496 (Pubitemid 20153653)
    • (1990) Biochemistry , vol.29 , Issue.18 , pp. 4490-4496
    • Williams, R.W.1    Starman, R.2    Taylor, K.M.P.3    Gable, K.4    Beeler, T.5    Zasloff, M.6    Covell, D.7
  • 60
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • B. Bechinger, M. Zasloff, and S.J. Opella Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy Protein Sci 2 1993 2077 2084 (Pubitemid 23354711)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 61
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • DOI 10.1016/0014-5793(89)81505-4
    • H.G. Boman, D. Wade, I.A. Boman, B. Whlin, and R.B. Merrifield Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids FEBS Lett 259 1989 103 106 (Pubitemid 20009957)
    • (1989) FEBS Letters , vol.259 , Issue.1 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wahlin, B.4    Merrifield, R.B.5
  • 62
    • 0020479083 scopus 로고
    • The structure of melittin. I. Structure determination and partial refinement
    • T.C. Terwilliger, and D. Eisenberg The structure of melittin. I. Structure determination and partial refinement J Biol Chem 257 1982 6010 6015
    • (1982) J Biol Chem , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 63
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • S. Frey, and L.K. Tamm Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study Biophys J 60 1991 922 930
    • (1991) Biophys J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 64
    • 0030048902 scopus 로고    scopus 로고
    • In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface
    • I. Cornut, B. Desbat, J.M. Turlet, and J. Dufourcq In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface Biophys J 70 1996 305 312 (Pubitemid 26021468)
    • (1996) Biophysical Journal , vol.70 , Issue.1 , pp. 305-312
    • Cornut, I.1    Desbat, B.2    Turlet, J.M.3    Dufourcq, J.4
  • 65
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat Rev Immunol 3 2003 710 720 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 67
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • DOI 10.1021/bi000714m
    • A. Rozek, C.L. Friedrich, and R.E.W. Hancock Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles Biochemistry 39 2000 15765 15774 (Pubitemid 32040945)
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.W.3
  • 68
    • 0035109873 scopus 로고    scopus 로고
    • Anti-microbial activity and cell binding are controled by sequence determinants in the anti-microbial peptide PR-39
    • DOI 10.1046/j.1523-1747.2001.01231.x
    • Y.R. Chan, M. Zanetti, R. Gennaro, and R.L. Gallo Anti-microbial activity and cell binding are controled by sequence determinants in the anti-microbial peptide PR-39 J Invest Dermatol 116 2001 230 235 (Pubitemid 32173726)
    • (2001) Journal of Investigative Dermatology , vol.116 , Issue.2 , pp. 230-235
    • Chan, Y.R.1    Zanetti, M.2    Gennaro, R.3    Gallo, R.L.4
  • 69
    • 0035112330 scopus 로고    scopus 로고
    • Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria
    • DOI 10.1128/IAI.69.3.1469-1476.2001
    • P.H. Nibbering, E. Ravensbergen, M.M. Welling, L.A. van Berkel, P.H.C. van Berkel, and E.K.J. Pauwels Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria Infect Immun 69 2001 1469 1476 (Pubitemid 32187596)
    • (2001) Infection and Immunity , vol.69 , Issue.3 , pp. 1469-1476
    • Nibbering, P.H.1    Ravensbergen, E.2    Welling, M.M.3    Van Berkel, L.A.4    Van Berkel, P.H.C.5    Pauwels, E.K.J.6    Nuijens, J.H.7
  • 70
    • 0348048803 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins (PGRPs)
    • DOI 10.1016/j.molimm.2003.10.011
    • R. Dziarski Peptidoglycan recognition proteins (PGRPs) Mol Immunol 40 2004 877 886 (Pubitemid 38032811)
    • (2004) Molecular Immunology , vol.40 , Issue.12 , pp. 877-886
    • Dziarski, R.1
  • 71
    • 31444440362 scopus 로고    scopus 로고
    • The peptidoglycan recognition protein PGRP-SC1a is essential for Toll signaling and phagocytosis of Staphylococcus aureus in Drosophila
    • DOI 10.1073/pnas.0506182103
    • L.S. Garver, J. Wu, and L.P. Wu The peptidoglycan recognition protein PGRP-SC1a is essential for Toll signaling and phagocytosis of Staphylococcus aureus in Drosophila Proc Natl Acad Sci USA 103 2006 660 665 (Pubitemid 43153082)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.3 , pp. 660-665
    • Garver, L.S.1    Wu, J.2    Wu, L.P.3
  • 73
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • DOI 10.1016/j.bbamem.2006.04.006, PII S0005273606001404
    • D.I. Chan, E.J. Prenner, and H.J. Vogel Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim Biophys Acta (BBA) - Biomembr 1758 2006 1184 1202 (Pubitemid 44444830)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 74
    • 79960087671 scopus 로고    scopus 로고
    • Lactoferrin: An iron-binding antimicrobial protein against Escherichia coli; Infection
    • C.-C. Yen, C.-J. Shen, W.-H. Hsu, Y.-H. Chang, H.-T. Lin, and H.-L. Chen Lactoferrin: an iron-binding antimicrobial protein against Escherichia coli; infection BioMetals 24 2011 585 594
    • (2011) BioMetals , vol.24 , pp. 585-594
    • Yen, C.-C.1    Shen, C.-J.2    Hsu, W.-H.3    Chang, Y.-H.4    Lin, H.-T.5    Chen, H.-L.6
  • 75
    • 0028273860 scopus 로고
    • Lactoferrin binds to porins OmpF and OmpC in Escherichia coli
    • J. Erdei, A. Forsgren, and A.S. Naidu Lactoferrin binds to porins OmpF and OmpC in Escherichia coli Infect Immun 62 1994 1236 1240 (Pubitemid 24110815)
    • (1994) Infection and Immunity , vol.62 , Issue.4 , pp. 1236-1240
    • Erdei, J.1    Forsgren, A.2    Naidu, A.S.3
  • 76
    • 0027531875 scopus 로고
    • Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium
    • S.S. Naidu, U. Svensson, A.R. Kishore, and A.S. Naidu Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium Antimicrob Agents Chemother 37 1993 240 245 (Pubitemid 23046562)
    • (1993) Antimicrobial Agents and Chemotherapy , vol.37 , Issue.2 , pp. 240-245
    • Naidu, S.S.1    Svensson, U.2    Kishore, A.R.3    Naidu, A.S.4
  • 77
    • 0033522876 scopus 로고    scopus 로고
    • Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin
    • F.R. Sallmann, S. Baveye-Descamps, F. Pattus, V. Salmon, N. Branza, and G. Spik Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin J Biol Chem 274 1999 16107 16114
    • (1999) J Biol Chem , vol.274 , pp. 16107-16114
    • Sallmann, F.R.1    Baveye-Descamps, S.2    Pattus, F.3    Salmon, V.4    Branza, N.5    Spik, G.6
  • 78
    • 0038397204 scopus 로고    scopus 로고
    • Lactoferricin derived from milk protein lactoferrin
    • DOI 10.2174/1381612033454829
    • H. Wakabayashi, M. Takase, and M. Tomita Lactoferricin derived from milk protein lactoferrin Curr Pharm Des 9 2003 1277 1287 (Pubitemid 36592136)
    • (2003) Current Pharmaceutical Design , vol.9 , Issue.16 , pp. 1277-1287
    • Wakabayashi, H.1    Takase, M.2    Tomita, M.3
  • 79
    • 0033787915 scopus 로고    scopus 로고
    • Antibacterial activity of 15-residue lactoferricin derivatives
    • M.B. Strøm, O. Rekdal, and J.S. Svendsen Antibacterial activity of 15-residue lactoferricin derivatives J Pept Res 56 2000 265 274
    • (2000) J Pept Res , vol.56 , pp. 265-274
    • Strøm, M.B.1    Rekdal, O.2    Svendsen, J.S.3
  • 80
    • 9644287934 scopus 로고    scopus 로고
    • The synthetic n-terminal peptide of human lactoferrin, hLF(1-11), is highly effective against experimental infection caused by multidrug-resistant Acinetobacter baumannii
    • DOI 10.1128/AAC.48.12.4919-4921.2004
    • L. Dijkshoorn, C.P.J.M. Brouwer, S.J.P. Bogaards, A. Nemec, P.J. van den Broek, and P.H. Nibbering The synthetic N-terminal peptide of human lactoferrin, hLF(1-11), is highly effective against experimental infection caused by multidrug-resistant acinetobacter baumannii Antimicrob Agents Chemother 48 2004 4919 4921 (Pubitemid 39577708)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.12 , pp. 4919-4921
    • Dijkshoorn, L.1    Brouwer, C.P.J.M.2    Bogaards, S.J.P.3    Nemec, A.4    Van Den Broek, P.J.5    Nibbering, P.H.6
  • 81
    • 0032847364 scopus 로고    scopus 로고
    • Antibacterial activity of multiple antigen peptides homologous to a loop region in human lactoferrin
    • DOI 10.1034/j.1399-3011.1999.00090.x
    • M. Azuma, C.A. Del Carpio, T. Kojima, I. Yokoyama, H. Tajiri, and K. Yoshikawa Antibacterial activity of multiple antigen peptides homologous to a loop region in human lactoferrin J Pept Res 54 1999 237 241 (Pubitemid 29444298)
    • (1999) Journal of Peptide Research , vol.54 , Issue.3 , pp. 237-241
    • Azuma, M.1    Kojima, T.2    Yokoyama, I.3    Tajiri, H.4    Yoshikawa, K.5    Saga, S.6    Del Carpio, C.A.7
  • 82
    • 77953289682 scopus 로고    scopus 로고
    • Bactericidal effect of bovine lactoferrin, LFcin, LFampin and LFchimera on antibiotic-resistant Staphylococcus aureus and Escherichia coli
    • H. Flores-Villaseñor, A. Canizalez-Román, M. Reyes-Lopez, K. Nazmi, M. de la Garza, and J. Zazueta-Beltrán Bactericidal effect of bovine lactoferrin, LFcin, LFampin and LFchimera on antibiotic-resistant Staphylococcus aureus and Escherichia coli Biometals 23 2010 569 578
    • (2010) Biometals , vol.23 , pp. 569-578
    • Flores-Villaseñor, H.1    Canizalez-Román, A.2    Reyes-Lopez, M.3    Nazmi, K.4    De La Garza, M.5    Zazueta-Beltrán, J.6
  • 83
    • 40849102416 scopus 로고    scopus 로고
    • Membrane curvature stress and antibacterial activity of lactoferricin derivatives
    • D. Zweytick, S. Tumer, S.E. Blondelle, and K. Lohner Membrane curvature stress and antibacterial activity of lactoferricin derivatives Biochem Biophys Res Commun 369 2008 395 400
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 395-400
    • Zweytick, D.1    Tumer, S.2    Blondelle, S.E.3    Lohner, K.4
  • 85
    • 58149127828 scopus 로고    scopus 로고
    • Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides
    • J.G.M. Bolscher, R. Adão, K. Nazmi, P.A.M. van den Keybus, W. van 't Hof, and A.V. Nieuw Amerongen Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides Biochimie 91 2009 123 132
    • (2009) Biochimie , vol.91 , pp. 123-132
    • Bolscher, J.G.M.1    Adão, R.2    Nazmi, K.3    Van Den Keybus, P.A.M.4    Van 'T Hof, W.5    Nieuw Amerongen, A.V.6
  • 87
    • 0036090558 scopus 로고    scopus 로고
    • Internal thiols and reactive oxygen species in candidacidal activity exerted by an N-terminal peptide of human lactoferrin
    • DOI 10.1128/AAC.46.6.1634-1639.2002
    • A. Lupetti, A. Paulusma-Annema, S. Senesi, M. Campa, J.T. van Dissel, and P.H. Nibbering Internal thiols and reactive oxygen species in candidacidal activity exerted by an N-terminal peptide of human lactoferrin Antimicrob Agents Chemother 46 2002 1634 1639 (Pubitemid 34535175)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.6 , pp. 1634-1639
    • Lupetti, A.1    Paulusma-Annema, A.2    Senesi, S.3    Campa, M.4    Van Dissel, J.T.5    Nibbering, P.H.6
  • 88
    • 0034916176 scopus 로고    scopus 로고
    • Packing characteristics of a model system mimicking cytoplasmic bacterial membranes
    • DOI 10.1016/S0009-3084(01)00157-8, PII S0009308401001578
    • K. Lohner, A. Latal, G. Degovics, and P. Garidel Packing characteristics of a model system mimicking cytoplasmic bacterial membranes Chem Phys Lipids 111 2001 177 192 (Pubitemid 32702027)
    • (2001) Chemistry and Physics of Lipids , vol.111 , Issue.2 , pp. 177-192
    • Lohner, K.1    Latal, A.2    Degovics, G.3    Garidel, P.4
  • 91
    • 21244475101 scopus 로고    scopus 로고
    • Phosphatidylethanolamine-phosphatidylglycerol bilayer as a model of the inner bacterial membrane
    • DOI 10.1529/biophysj.104.048835
    • K. Murzyn, T. Róg, and M. Pasenkiewicz-Gierula Phosphatidylethanolamine-phosphatidylglycerol bilayer as a model of the inner bacterial membrane Biophys J 88 2005 1091 1103 (Pubitemid 40975941)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1091-1103
    • Murzyn, K.1    Rog, T.2    Pasenkiewicz-Gierula, M.3
  • 92
    • 44449167975 scopus 로고    scopus 로고
    • Role of phosphatidylglycerols in the stability of bacterial membranes
    • W. Zhao, T. Róg, A.A. Gurtovenko, I. Vattulainen, and M. Karttunen Role of phosphatidylglycerols in the stability of bacterial membranes Biochimie 90 2008 930 938
    • (2008) Biochimie , vol.90 , pp. 930-938
    • Zhao, W.1    Róg, T.2    Gurtovenko, A.A.3    Vattulainen, I.4    Karttunen, M.5
  • 93
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as predictors of antimicrobial potency
    • R.M. Epand, S. Rotem, A. Mor, B. Berno, and R.F. Epand Bacterial membranes as predictors of antimicrobial potency J Am Chem Soc 130 2008 14346 14352
    • (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
  • 94
    • 67349231331 scopus 로고    scopus 로고
    • The interactions between phosphatidylglycerol and phosphatidylethanolamines in model bacterial membranes: The effect of the acyl chain length and saturation
    • P. Wydro, and K. Witkowska The interactions between phosphatidylglycerol and phosphatidylethanolamines in model bacterial membranes: The effect of the acyl chain length and saturation Colloids Surf B: Biointerfaces 72 2009 32 39
    • (2009) Colloids Surf B: Biointerfaces , vol.72 , pp. 32-39
    • Wydro, P.1    Witkowska, K.2
  • 95
    • 78650159655 scopus 로고    scopus 로고
    • Influence of lysine N-trimethylation and lipid composition on the membrane activity of the cecropin A-melittin hybrid peptide CA(1-7)M(2-9)
    • V. Teixeira, M.J. Feio, L. Rivas, B.G. De la Torre, D. Andreu, and A. Coutinho Influence of lysine N-trimethylation and lipid composition on the membrane activity of the cecropin A-melittin hybrid peptide CA(1-7)M(2-9) J Phys Chem B 114 2010 16198 16208
    • (2010) J Phys Chem B , vol.114 , pp. 16198-16208
    • Teixeira, V.1    Feio, M.J.2    Rivas, L.3    De La Torre, B.G.4    Andreu, D.5    Coutinho, A.6
  • 96
    • 60549086215 scopus 로고    scopus 로고
    • Peptide induced demixing in PG/PE lipid mixtures: A mechanism for the specificity of antimicrobial peptides towards bacterial membranes?
    • A. Arouri, M. Dathe, and A. Blume Peptide induced demixing in PG/PE lipid mixtures: a mechanism for the specificity of antimicrobial peptides towards bacterial membranes? Biochim Biophys Acta (BBA) - Biomembr 1788 2008 650 659
    • (2008) Biochim Biophys Acta (BBA) - Biomembr , vol.1788 , pp. 650-659
    • Arouri, A.1    Dathe, M.2    Blume, A.3
  • 97
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • DOI 10.1074/jbc.M203186200
    • H. Zhao, and P.K.J. Kinnunen Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence J Biol Chem 277 2002 25170 25177 (Pubitemid 34951823)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.J.2
  • 98
    • 73949132404 scopus 로고    scopus 로고
    • High potency and broad-spectrum antimicrobial peptides synthesized via ring-opening polymerization of α-aminoacid-N-carboxyanhydrides
    • C. Zhou, X. Qi, P. Li, W.N. Chen, L. Mouad, and M.W. Chang High potency and broad-spectrum antimicrobial peptides synthesized via ring-opening polymerization of α-aminoacid-N-carboxyanhydrides Biomacromolecules 11 2009 60 67
    • (2009) Biomacromolecules , vol.11 , pp. 60-67
    • Zhou, C.1    Qi, X.2    Li, P.3    Chen, W.N.4    Mouad, L.5    Chang, M.W.6
  • 99
    • 15244358803 scopus 로고    scopus 로고
    • Interaction of melittin with membrane cholesterol: A fluorescence approach
    • DOI 10.1529/biophysj.104.043596
    • H. Raghuraman, and A. Chattopadhyay Interaction of melittin with membrane cholesterol: a fluorescence approach Biophys J 87 2004 2419 2432 (Pubitemid 41071340)
    • (2004) Biophysical Journal , vol.87 , Issue.4 , pp. 2419-2432
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 100
    • 0031027375 scopus 로고    scopus 로고
    • Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: A property used for membrane targeting
    • DOI 10.1007/s002490050032
    • T. Benachir, M. Monette, J. Grenier, and M. Lafleur Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: a property used for membrane targeting Eur Biophys J 25 1997 201 210 (Pubitemid 27055919)
    • (1997) European Biophysics Journal , vol.25 , Issue.3 , pp. 201-210
    • Benachir, T.1    Monette, M.2    Grenier, J.3    Lafleur, M.4
  • 101
    • 41549110793 scopus 로고    scopus 로고
    • Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells
    • H. Suttmann, M. Retz, F. Paulsen, J. Harder, U. Zwergel, and J. Kamradt Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells BMC Urol 8 2008 5
    • (2008) BMC Urol , vol.8 , pp. 5
    • Suttmann, H.1    Retz, M.2    Paulsen, F.3    Harder, J.4    Zwergel, U.5    Kamradt, J.6
  • 103
    • 33645457007 scopus 로고    scopus 로고
    • Elevated levels of cholesterol-rich lipid rafts in cancer cells are correlated with apoptosis sensitivity induced by cholesterol-depleting agents
    • Y.C. Li, M.J. Park, S.-K. Ye, C.-W. Kim, and Y.-N. Kim Elevated levels of cholesterol-rich lipid rafts in cancer cells are correlated with apoptosis sensitivity induced by cholesterol-depleting agents Am J Pathol 168 2006 1107 1118
    • (2006) Am J Pathol , vol.168 , pp. 1107-1118
    • Li, Y.C.1    Park, M.J.2    Ye, S.-K.3    Kim, C.-W.4    Kim, Y.-N.5
  • 104
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • D. Andreu, and L. Rivas Animal antimicrobial peptides: an overview Pept Sci 47 1998 415 433
    • (1998) Pept Sci , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 105
    • 25444466265 scopus 로고    scopus 로고
    • Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition
    • DOI 10.1021/jp051572e
    • F. Abrunhosa, S. Faria, P. Gomes, I. Tomaz, J.C. Pessoa, and D. Andreu Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition J Phys Chem B 109 2005 17311 17319 (Pubitemid 41361410)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.36 , pp. 17311-17319
    • Abrunhosa, F.1    Faria, S.2    Gomes, P.3    Tomaz, I.4    Pessoa, J.C.5    Andreu, D.6    Bastos, M.7
  • 106
    • 44049094436 scopus 로고    scopus 로고
    • Energetics and partition of two cecropin-melittin hybrid peptides to model membranes of different composition
    • M. Bastos, G. Bai, P. Gomes, D. Andreu, E. Goormaghtigh, and M. Prieto Energetics and partition of two cecropin-melittin hybrid peptides to model membranes of different composition Biophys J 94 2008 2128 2141
    • (2008) Biophys J , vol.94 , pp. 2128-2141
    • Bastos, M.1    Bai, G.2    Gomes, P.3    Andreu, D.4    Goormaghtigh, E.5    Prieto, M.6
  • 107
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • DOI 10.1021/bi00436a014
    • E. Kuchinka, and J. Seelig Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation Biochemistry 28 1989 4216 4221 (Pubitemid 19141622)
    • (1989) Biochemistry , vol.28 , Issue.10 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 108
    • 0345017115 scopus 로고    scopus 로고
    • The hemolytic activity of six arachnid cationic peptides is affected by the phosphatidylcholine-to-sphingomyelin ratio in lipid bilayers
    • DOI 10.1016/j.bbamem.2003.08.010
    • O.S. Belokoneva, E. Villegas, G. Corzo, L. Dai, and T. Nakajima The hemolytic activity of six arachnid cationic peptides is affected by the phosphatidylcholine-to-sphingomyelin ratio in lipid bilayers Biochim Biophys Acta (BBA) - Biomembr 1617 2003 22 30 (Pubitemid 37456709)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1617 , Issue.1-2 , pp. 22-30
    • Belokoneva, O.S.1    Villegas, E.2    Corzo, G.3    Dai, L.4    Nakajima, T.5
  • 109
    • 34047249400 scopus 로고    scopus 로고
    • Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation
    • DOI 10.1016/j.bbamem.2007.02.005, PII S0005273607000405
    • M.N. Melo, and M.A.R.B. Castanho Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation Biochim Biophys Acta (BBA) - Biomembr 1768 2007 1277 1290 (Pubitemid 46550363)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.5 , pp. 1277-1290
    • Melo, M.N.1    Castanho, M.A.R.B.2
  • 110
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the [alpha]-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Thermodynamics of the [alpha]-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium J Mol Biol 294 1999 785 794
    • (1999) J Mol Biol , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 112
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • DOI 10.1016/j.bbamem.2004.08.004, PII S0005273604002056, Lipid-Protein Interactions
    • J. Seelig Thermodynamics of lipid-peptide interactions Biochim Biophys Acta (BBA) - Biomembr 1666 2004 40 50 (Pubitemid 39425197)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 40-50
    • Seelig, J.1
  • 113
    • 32544456244 scopus 로고    scopus 로고
    • Antimicrobial peptides: New candidates in the fight against bacterial infections
    • DOI 10.1002/bip.20286
    • O. Toke Antimicrobial peptides: new candidates in the fight against bacterial infections Pept Sci 80 2005 717 735 (Pubitemid 43266580)
    • (2005) Biopolymers - Peptide Science Section , vol.80 , Issue.6 , pp. 717-735
    • Toke, O.1
  • 114
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Y. Chen, C.T. Mant, S.W. Farmer, R.E.W. Hancock, M.L. Vasil, and R.S. Hodges Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index J Biol Chem 280 2005 12316 12329
    • (2005) J Biol Chem , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 115
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • DOI 10.1021/bi962507l
    • Z. Oren, and Y. Shai Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study Biochemistry 36 1997 1826 1835 (Pubitemid 27086279)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 116
    • 0029665072 scopus 로고    scopus 로고
    • Diastereomers of cytolysins, a novel class of potent antibacterial peptides
    • DOI 10.1074/jbc.271.13.7305
    • Y. Shai, and Z. Oren Diastereomers of cytolysins, a novel class of potent antibacterial peptides J Biol Chem 271 1996 7305 7308 (Pubitemid 26106994)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.13 , pp. 7305-7308
    • Shai, Y.1    Oren, Z.2
  • 117
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • DOI 10.1021/bi960835f
    • M. Dathe, M. Schumann, T. Wieprecht, A. Winkler, M. Beyermann, and E. Krause Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes Biochemistry 35 1996 12612 12622 (Pubitemid 26318059)
    • (1996) Biochemistry , vol.35 , Issue.38 , pp. 12612-12622
    • Datrie, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 118
    • 0026533988 scopus 로고
    • Augmentation of the antibacterial activity of magainin by positive-charge chain extension
    • R. Bessalle, H. Haas, A. Goria, I. Shalit, and M. Fridkin Augmentation of the antibacterial activity of magainin by positive-charge chain extension Antimicrob Agents Chemother 36 1992 313 317
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 313-317
    • Bessalle, R.1    Haas, H.2    Goria, A.3    Shalit, I.4    Fridkin, M.5
  • 119
    • 3042781052 scopus 로고    scopus 로고
    • Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology
    • S.H. Marshall, and G. Arenas Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology Electronic J Biotechnol 6 2003 271 284
    • (2003) Electronic J Biotechnol , vol.6 , pp. 271-284
    • Marshall, S.H.1    Arenas, G.2
  • 120
    • 73549121068 scopus 로고    scopus 로고
    • Anionic antimicrobial peptides from eukaryotic organisms
    • F. Harris, S.R. Dennison, and D.A. Phoenix Anionic antimicrobial peptides from eukaryotic organisms Curr Protein Pept Sci 10 2009 585 606
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 585-606
    • Harris, F.1    Dennison, S.R.2    Phoenix, D.A.3
  • 122
    • 0030664760 scopus 로고    scopus 로고
    • Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
    • DOI 10.1016/S0014-5793(97)01266-0, PII S0014579397012660
    • T. Wieprecht, M. Dathe, E. Krause, M. Beyermann, W.L. Maloy, and D.L. MacDonald Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment FEBS Lett 417 1997 135 140 (Pubitemid 27490489)
    • (1997) FEBS Letters , vol.417 , Issue.1 , pp. 135-140
    • Wieprecht, T.1    Dathe, M.2    Krause, E.3    Beyermann, M.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 123
    • 84857239252 scopus 로고    scopus 로고
    • Modulation of specificity in cyclic antimicrobial peptides by amphipathicity
    • G.B. Fields, J.P. Tam, G. Barany, Springer Netherlands Netherlands
    • L. Kondejewski, C. McInnes, M. Jelokhani-Niaraki, S. Farmer, C. Kay, and B. Sykes Modulation of specificity in cyclic antimicrobial peptides by amphipathicity G.B. Fields, J.P. Tam, G. Barany, Peptides for the New Millennium 2002 Springer Netherlands Netherlands 752 753
    • (2002) Peptides for the New Millennium , pp. 752-753
    • Kondejewski, L.1    McInnes, C.2    Jelokhani-Niaraki, M.3    Farmer, S.4    Kay, C.5    Sykes, B.6
  • 124
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • DOI 10.1128/AAC.46.11.3585-3590.2002
    • M. Stark, L.-P. Liu, and C.M. Deber Cationic hydrophobic peptides with antimicrobial activity Antimicrob Agents Chemother 46 2002 3585 3590 (Pubitemid 35192930)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.11 , pp. 3585-3590
    • Stark, M.1    Liu, L.-P.2    Deber, C.M.3
  • 125
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides
    • DOI 10.1128/AAC.00925-06
    • Y. Chen, M.T. Guarnieri, A.I. Vasil, M.L. Vasil, C.T. Mant, and R.S. Hodges Role of peptide hydrophobicity in the mechanism of action of [alpha]-helical antimicrobial peptides Antimicrob Agents Chemother 51 2007 1398 1406 (Pubitemid 46586822)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.4 , pp. 1398-1406
    • Chen, Y.1    Guarnieri, M.T.2    Vasil, A.I.3    Vasil, M.L.4    Mant, C.T.5    Hodges, R.S.6
  • 126
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • H.-T. Chou, T.-Y. Kuo, J.-C. Chiang, M.-J. Pei, W.-T. Yang, and H.-C. Yu Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp Int J Antimicrob Agents 32 2008 130 138
    • (2008) Int J Antimicrob Agents , vol.32 , pp. 130-138
    • Chou, H.-T.1    Kuo, T.-Y.2    Chiang, J.-C.3    Pei, M.-J.4    Yang, W.-T.5    Yu, H.-C.6
  • 127
    • 0037016737 scopus 로고    scopus 로고
    • Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework
    • DOI 10.1074/jbc.M107825200
    • L.H. Kondejewski, D.L. Lee, M. Jelokhani-Niaraki, S.W. Farmer, R.E.W. Hancock, and R.S. Hodges Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework J Biol Chem 277 2002 67 74 (Pubitemid 34952029)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 67-74
    • Kondejewski, L.H.1    Lee, D.L.2    Jelokhani-Niaraki, M.3    Farmer, S.W.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 128
    • 12544259357 scopus 로고    scopus 로고
    • Structure-activity relationships of diastereomeric lysine ring size analogs of the antimicrobial peptide gramicidin S
    • E.J. Prenner, M. Kiricsi, M. Jelokhani-Niaraki, R.N.A.H. Lewis, R.S. Hodges, and R.N. McElhaney Structure-activity relationships of diastereomeric lysine ring size analogs of the antimicrobial peptide gramicidin S J Biol Chem 280 2005 2002 2011
    • (2005) J Biol Chem , vol.280 , pp. 2002-2011
    • Prenner, E.J.1    Kiricsi, M.2    Jelokhani-Niaraki, M.3    Lewis, R.N.A.H.4    Hodges, R.S.5    McElhaney, R.N.6
  • 129
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • M. Dathe, and T. Wieprecht Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells Biochim Biophys Acta (BBA) - Biomembr 1462 1999 71 87
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 130
    • 0033799243 scopus 로고    scopus 로고
    • Polar angle as a determinant of amphipathic [alpha]-helix-lipid interactions: A model peptide study
    • N. Uematsu, and K. Matsuzaki Polar angle as a determinant of amphipathic [alpha]-helix-lipid interactions: a model peptide study Biophys J 79 2000 2075 2083
    • (2000) Biophys J , vol.79 , pp. 2075-2083
    • Uematsu, N.1    Matsuzaki, K.2
  • 131
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • DOI 10.1016/S0014-5793(97)00055-0, PII S0014579397000550
    • M. Dathe, T. Wieprecht, H. Nikolenko, L. Handel, W.L. Maloy, and D.L. MacDonald Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides FEBS Lett 403 1997 208 212 (Pubitemid 27081496)
    • (1997) FEBS Letters , vol.403 , Issue.2 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    MacDonald, D.L.6    Beyermann, M.7    Bienert, M.8
  • 132
    • 33645780418 scopus 로고    scopus 로고
    • The antimicrobial peptide polyphemusin localizes to the cytoplasm of Escherichia coli following treatment
    • J.-P.S. Powers, M.M. Martin, D.L. Goosney, and R.E.W. Hancock The antimicrobial peptide polyphemusin localizes to the cytoplasm of Escherichia coli following treatment Antimicrob Agents Chemother 50 2006 1522 1524
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1522-1524
    • Powers, J.-P.S.1    Martin, M.M.2    Goosney, D.L.3    Hancock, R.E.W.4
  • 133
    • 0033569408 scopus 로고    scopus 로고
    • [Beta]-defensins: Linking innate and adaptive immunity through dendritic and T cell CCR6
    • D. Yang, O. Chertov, S.N. Bykovskaia, Q. Chen, M.J. Buffo, and J. Shogan [Beta]-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6 Science 286 1999 525 528
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1    Chertov, O.2    Bykovskaia, S.N.3    Chen, Q.4    Buffo, M.J.5    Shogan, J.6
  • 134
    • 11244335404 scopus 로고    scopus 로고
    • Studies on the cellular uptake of substance P and lysine-rich, KLA-derived model peptides
    • DOI 10.1002/jmr.691
    • J. Oehlke, D. Lorenz, B. Wiesner, and M. Bienert Studies on the cellular uptake of substance P and lysine-rich, KLA-derived model peptides J Mol Recognit 18 2005 50 59 (Pubitemid 40059570)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.1 , pp. 50-59
    • Oehlke, J.1    Lorenz, D.2    Wiesner, B.3    Bienert, M.4
  • 135
    • 25844437587 scopus 로고    scopus 로고
    • Atomic force microscopy study of the effect of antimicrobial peptides on the cell envelope of Escherichia coli
    • DOI 10.1128/AAC.49.10.4085-4092.2005
    • M. Meincken, D.L. Holroyd, and M. Rautenbach Atomic force microscopy study of the effect of antimicrobial peptides on the cell envelope of Escherichia coli Antimicrob Agents Chemother 49 2005 4085 4092 (Pubitemid 41400950)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.10 , pp. 4085-4092
    • Meincken, M.1    Holroyd, D.L.2    Rautenbach, M.3
  • 136
    • 0037100360 scopus 로고    scopus 로고
    • The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study
    • D. Grasso, D. Milardi, C.L. Rosa, G. Impellizzeri, and G. Pappalardo The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study Thermochim Acta 390 2002 73 78
    • (2002) Thermochim Acta , vol.390 , pp. 73-78
    • Grasso, D.1    Milardi, D.2    Rosa, C.L.3    Impellizzeri, G.4    Pappalardo, G.5
  • 137
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Lipid domains in bacterial membranes and the action of antimicrobial agents Biochim Biophys Acta (BBA) - Biomembr 1788 2009 289 294
    • (2009) Biochim Biophys Acta (BBA) - Biomembr , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 138
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • DOI 10.1016/S0140-6736(97)80051-7
    • R.E.W. Hancock Peptide antibiotics Lancet 349 1997 418 422 (Pubitemid 27077684)
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 140
    • 33847019613 scopus 로고    scopus 로고
    • Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria
    • DOI 10.1016/j.bbamem.2006.12.010, PII S0005273606004858
    • A. Li, P.Y. Lee, B. Ho, J.L. Ding, and C.T. Lim Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria Biochim Biophys Acta (BBA) - Biomembr 1768 2007 411 418 (Pubitemid 46275606)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.3 , pp. 411-418
    • Li, A.1    Lee, P.Y.2    Ho, B.3    Ding, J.L.4    Lim, C.T.5
  • 141
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wail precursor lipid II by a pore-forming peptide antibiotic
    • DOI 10.1126/science.286.5448.2361
    • E. Breukink, I. Wiedemann, Cv. Kraaij, O.P. Kuipers, H.-G. Sahl, and B. de Kruijff Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic Science 286 1999 2361 2364 (Pubitemid 30016902)
    • (1999) Science , vol.286 , Issue.5448 , pp. 2361-2364
    • Breukink, E.1    Wiedemann, I.2    Van Kraaij, C.3    Kuipers, O.P.4    Sahl, H.-G.5    De Kruijff, B.6
  • 145
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • DOI 10.1016/0005-2736(94)90050-7
    • S.J. Ludtke, K. He, Y. Wu, and H.W. Huang Cooperative membrane insertion of magainin correlated with its cytolytic activity Biochim Biophys Acta (BBA) - Biomembr 1190 1994 181 184 (Pubitemid 24066276)
    • (1994) Biochimica et Biophysica Acta - Biomembranes , vol.1190 , Issue.1 , pp. 181-184
    • Ludtke, S.J.1    He, K.2    Wu, Y.3    Huang, H.W.4
  • 146
    • 0031006189 scopus 로고    scopus 로고
    • Effect of changing the size of lipid headgroup on peptide insertion into membranes
    • W.T. Heller, K. He, S.J. Ludtke, T.A. Harroun, and H.W. Huang Effect of changing the size of lipid headgroup on peptide insertion into membranes Biophys J 73 1997 239 244 (Pubitemid 27274121)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 239-244
    • Heller, W.T.1    He, K.2    Ludtke, S.J.3    Harroun, T.A.4    Huang, H.W.5
  • 148
    • 37349002470 scopus 로고    scopus 로고
    • Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization
    • DOI 10.1529/biophysj.107.116681
    • A.J. Mason, A. Marquette, and B. Bechinger Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization Biophys J 93 2007 4289 4299 (Pubitemid 350294476)
    • (2007) Biophysical Journal , vol.93 , Issue.12 , pp. 4289-4299
    • Mason, A.J.1    Marquette, A.2    Bechinger, B.3
  • 149
    • 68749115077 scopus 로고    scopus 로고
    • Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape
    • B. Bechinger Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape Curr Opin Colloid Interf Sci 14 2009 349 355
    • (2009) Curr Opin Colloid Interf Sci , vol.14 , pp. 349-355
    • Bechinger, B.1
  • 150
    • 28444488982 scopus 로고    scopus 로고
    • Many-body effect of antimicrobial peptides: On the correlation between lipid's spontaneous curvature and pore formation
    • DOI 10.1529/biophysj.105.068080
    • M.-T. Lee, W.-C. Hung, F.-Y. Chen, and H.W. Huang Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formation Biophys J 89 2005 4006 4016 (Pubitemid 41725621)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4006-4016
    • Lee, M.-T.1    Hung, W.-C.2    Chen, F.-Y.3    Huang, H.W.4
  • 151
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation
    • G. Klocek, T. Schulthess, Y. Shai, and J. Seelig Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation Biochemistry 48 2009 2586 2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 152
    • 0025996974 scopus 로고    scopus 로고
    • Nonclassical hydrophobic effect in membrane binding equilibria
    • J. Seelig, and P. Ganz Nonclassical hydrophobic effect in membrane binding equilibria Biochemistry 30 2002 9354 9359
    • (2002) Biochemistry , vol.30 , pp. 9354-9359
    • Seelig, J.1    Ganz, P.2
  • 154
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • W.C. Wimley, and S.H. White Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat Struct Mol Biol 3 1996 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 157
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • J.M. Scholtz, H. Qian, E.J. York, J.M. Stewart, and R.L. Baldwin Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water Biopolymers 31 1991 1463 1470
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 158
    • 0035282941 scopus 로고    scopus 로고
    • Thermodynamics of the helix-coil transition: Binding of S15 and a hybrid sequence, disulfide stabilized peptide to the S-protein
    • DOI 10.1002/1097-0134(20010301)42:4<523::AID-PROT100>3.0.CO;2-B
    • M. Bastos, J.H.B. Pease, D.E. Wemmer, K.P. Murphy, and P.R. Connelly Thermodynamics of the helix-coil transition: Binding of S15 and a hybrid sequence, disulfide stabilized peptide to the S-protein Proteins: Struct Funct Bioinform 42 2001 523 530 (Pubitemid 32179861)
    • (2001) Proteins: Structure, Function and Genetics , vol.42 , Issue.4 , pp. 523-530
    • Bastos, M.1    Pease, J.H.B.2    Wemmer, D.E.3    Murphy, K.P.4    Connelly, P.R.5
  • 159
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • DOI 10.1016/S0304-4157(98)00021-5, PII S0304415798000215
    • S.H. White, and W.C. Wimley Hydrophobic interactions of peptides with membrane interfaces Biochim Biophys Acta (BBA) - Rev Biomembr 1376 1998 339 352 (Pubitemid 28517884)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 160
    • 0034719492 scopus 로고    scopus 로고
    • Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-β strand cystine knot framework
    • DOI 10.1006/bbrc.1999.2035
    • J.P. Tam, Y.-A. Lu, and J.-L. Yang Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-[beta] strand cystine knot framework Biochem Biophys Res Commun 267 2000 783 790 (Pubitemid 30099401)
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , Issue.3 , pp. 783-790
    • Tam, J.P.1    Lu, Y.-A.2    Yang, J.-L.3
  • 161
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • B. Christensen, J. Fink, R.B. Merrifield, and D. Mauzerall Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes Proc Natl Acad Sci USA 85 1988 5072 5076
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 162
    • 17844400564 scopus 로고    scopus 로고
    • Mechanism of membrane activity of the antibiotic trichogin GA IV: A two-state transition controlled by peptide concentration
    • DOI 10.1529/biophysj.104.056077
    • C. Mazzuca, L. Stella, M. Venanzi, F. Formaggio, C. Toniolo, and B. Pispisa Mechanism of membrane activity of the antibiotic trichogin GA IV: a two-state transition controlled by peptide concentration Biophys J 88 2005 3411 3421 (Pubitemid 40586591)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3411-3421
    • Mazzuca, C.1    Stella, L.2    Venanzi, M.3    Formaggio, F.4    Toniolo, C.5    Pispisa, B.6
  • 163
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic [alpha]-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
    • A.K. Mahalka, and P.K.J. Kinnunen Binding of amphipathic [alpha]-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L Biochim Biophys Acta (BBA) - Biomembr 1788 2009 1600 1609
    • (2009) Biochim Biophys Acta (BBA) - Biomembr , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.J.2
  • 164
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action
    • DOI 10.1016/j.bbamem.2006.03.037, PII S0005273606001982
    • H. Zhao, R. Sood, A. Jutila, S. Bose, G. Fimland, and J. Nissen-Meyer Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action Biochim Biophys Acta (BBA) - Biomembr 1758 2006 1461 1474 (Pubitemid 44436085)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5    Nissen-Meyer, J.6    Kinnunen, P.K.J.7
  • 165
    • 36048946958 scopus 로고    scopus 로고
    • A novel technique to study pore-forming peptides in a natural membrane
    • DOI 10.1007/s00249-007-0152-4, Proceedings of the XVIII Congress of the Italian Society of Pure and Applied Biophysics (SIBPA), Palermo, Sicily, September 2006
    • N. Vedovato, and G. Rispoli A novel technique to study pore-forming peptides in a natural membrane Eur Biophys J 36 2007 771 778 (Pubitemid 350092511)
    • (2007) European Biophysics Journal , vol.36 , Issue.7 , pp. 771-778
    • Vedovato, N.1    Rispoli, G.2
  • 167
    • 0015760624 scopus 로고
    • The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes
    • M. Eisenberg, J.E. Hall, and C.A. Mead The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes J Membr Biol 14 1973 143 176
    • (1973) J Membr Biol , vol.14 , pp. 143-176
    • Eisenberg, M.1    Hall, J.E.2    Mead, C.A.3
  • 169
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by [alpha]-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai 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 (BBA) - Biomembr 1462 1999 55 70
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 170
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • S. Yamaguchi, D. Huster, A. Waring, R.I. Lehrer, W. Kearney, and B.F. Tack Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy Biophys J 81 2001 2203 2214 (Pubitemid 32917169)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 171
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides
    • DOI 10.1021/bi0267846
    • N. Papo, and Y. Shai Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides Biochemistry 42 2002 458 466 (Pubitemid 36105764)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 172
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • N. Sitaram, and R. Nagaraj Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity Biochim Biophys Acta (BBA) - Biomembr 1462 1999 29 54
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 174
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • DOI 10.1021/bi9630826
    • L. Silvestro, K. Gupta, J.N. Weiser, and P.H. Axelsen The concentration-dependent membrane activity of cecropin A Biochemistry 36 1997 11452 11460 (Pubitemid 27408628)
    • (1997) Biochemistry , vol.36 , Issue.38 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 175
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • M. Wu, E. Maier, R. Benz, and R.E.W. Hancock Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli Biochemistry 38 1999 7235 7242
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 176
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: A unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • M. Miteva, M. Andersson, A. Karshikoff, and G. Otting Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin FEBS Lett 462 1999 155 158
    • (1999) FEBS Lett , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 179
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles
    • DOI 10.1021/bi020244r
    • A. Pokorny, T.H. Birkbeck, and P.F.F. Almeida Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles Biochemistry 41 2002 11044 11056 (Pubitemid 35001219)
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 180
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides
    • DOI 10.1021/bi0497087
    • A. Pokorny, and P.F.F. Almeida Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides Biochemistry 43 2004 8846 8857 (Pubitemid 38880055)
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 181
    • 21844443548 scopus 로고    scopus 로고
    • Permeabilization of raft-containing lipid vesicles by δ-lysin: A mechanism for cell sensitivity to cytotoxic peptides
    • DOI 10.1021/bi0506371
    • A. Pokorny, and P.F.F. Almeida Permeabilization of raft-containing lipid vesicles by δ-lysin: a mechanism for cell sensitivity to cytotoxic peptides Biochemistry 44 2005 9538 9544 (Pubitemid 40962052)
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9538-9544
    • Pokorny, A.1    Almeida, P.F.F.2
  • 182
    • 71649106004 scopus 로고    scopus 로고
    • Induction of non-lamellar lipid phases by antimicrobial peptides: A potential link to mode of action
    • E.F. Haney, S. Nathoo, H.J. Vogel, and E.J. Prenner Induction of non-lamellar lipid phases by antimicrobial peptides: a potential link to mode of action Chem Phys Lipids 163 2010 82 93
    • (2010) Chem Phys Lipids , vol.163 , pp. 82-93
    • Haney, E.F.1    Nathoo, S.2    Vogel, H.J.3    Prenner, E.J.4
  • 183
    • 77952362863 scopus 로고    scopus 로고
    • Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: Lipid clustering in anionic membranes
    • R.F. Epand, L. Maloy, A. Ramamoorthy, and R.M. Epand Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: lipid clustering in anionic membranes Biophys J 98 2010 2564 2573
    • (2010) Biophys J , vol.98 , pp. 2564-2573
    • Epand, R.F.1    Maloy, L.2    Ramamoorthy, A.3    Epand, R.M.4
  • 185
    • 70349119495 scopus 로고    scopus 로고
    • Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37
    • R.F. Epand, G. Wang, B. Berno, and R.M. Epand Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37 Antimicrob Agents Chemother 53 2009 3705 3714
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 3705-3714
    • Epand, R.F.1    Wang, G.2    Berno, B.3    Epand, R.M.4
  • 187
    • 5644241027 scopus 로고    scopus 로고
    • Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity
    • DOI 10.1111/j.1365-2443.2004.00782.x
    • K. Iwamoto, S. Kobayashi, R. Fukuda, M. Umeda, T. Kobayashi, and A. Ohta Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity Genes Cells 9 2004 891 903 (Pubitemid 39369022)
    • (2004) Genes to Cells , vol.9 , Issue.10 , pp. 891-903
    • Iwamoto, K.1    Kobayashi, S.2    Fukuda, R.3    Umeda, M.4    Kobayashi, T.5    Ohta, A.6
  • 188
    • 14644412812 scopus 로고    scopus 로고
    • Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
    • DOI 10.1128/JB.187.6.2163-2174.2005
    • A. Nishibori, J. Kusaka, H. Hara, M. Umeda, and K. Matsumoto Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes J Bacteriol 187 2005 2163 2174 (Pubitemid 40316247)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2163-2174
    • Nishibori, A.1    Kusaka, J.2    Hara, H.3    Umeda, M.4    Matsumoto, K.5
  • 189
    • 0034640856 scopus 로고    scopus 로고
    • An essential role for a membrane lipid in cytokinesis: Regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine
    • DOI 10.1083/jcb.149.6.1215
    • K. Emoto, and M. Umeda An essential role for a membrane lipid in cytokinesis: regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine J Cell Biol 149 2000 1215 1224 (Pubitemid 30399675)
    • (2000) Journal of Cell Biology , vol.149 , Issue.6 , pp. 1215-1224
    • Emoto, K.1    Umeda, M.2
  • 190
    • 0035424718 scopus 로고    scopus 로고
    • Implications of lipid microdomains for membrane curvature, budding and fission: Commentary
    • DOI 10.1016/S0955-0674(00)00239-8
    • W.B. Huttner, and J. Zimmerberg Implications of lipid microdomains for membrane curvature, budding and fission: commentary Curr Opin Cell Biol 13 2001 478 484 (Pubitemid 32709772)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.4 , pp. 478-484
    • Huttner, W.B.1    Zimmerberg, J.2
  • 191
    • 33747038638 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes
    • DOI 10.1111/j.1365-2958.2006.05317.x
    • K. Matsumoto, J. Kusaka, A. Nishibori, and H. Hara Lipid domains in bacterial membranes Mol Microbiol 61 2006 1110 1117 (Pubitemid 44215416)
    • (2006) Molecular Microbiology , vol.61 , Issue.5 , pp. 1110-1117
    • Matsumoto, K.1    Kusaka, J.2    Nishibori, A.3    Hara, H.4
  • 192
    • 77951253196 scopus 로고    scopus 로고
    • Designed low amphipathic peptides with [alpha]-helical propensity exhibiting antimicrobial activity via a lipid domain formation mechanism
    • N. Yamamoto, and A. Tamura Designed low amphipathic peptides with [alpha]-helical propensity exhibiting antimicrobial activity via a lipid domain formation mechanism Peptides 5 2010 794 805
    • (2010) Peptides , vol.5 , pp. 794-805
    • Yamamoto, N.1    Tamura, A.2
  • 193
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • DOI 10.1038/nature02621
    • M.P. Mattson Pathways towards and away from Alzheimer's disease Nature 430 2004 631 639 (Pubitemid 39061671)
    • (2004) Nature , vol.430 , Issue.7000 , pp. 631-639
    • Mattson, M.P.1
  • 194
    • 0035118091 scopus 로고    scopus 로고
    • Hypothesis: Membrane domains and hyperstructures control bacterial division
    • DOI 10.1016/S0300-9084(00)01203-7
    • V. Norris, and I. Fishov Hypothesis: membrane domains and hyperstructures control bacterial division Biochimie 83 2001 91 97 (Pubitemid 32181529)
    • (2001) Biochimie , vol.83 , Issue.1 , pp. 91-97
    • Norris, V.1    Fishov, I.2
  • 195
    • 0036050398 scopus 로고    scopus 로고
    • The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • DOI 10.1046/j.1365-2958.2002.02993.x
    • C.L. Woldringh The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation Mol Microbiol 45 2002 17 29 (Pubitemid 35025930)
    • (2002) Molecular Microbiology , vol.45 , Issue.1 , pp. 17-29
    • Woldringh, C.L.1
  • 196
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • J. Rossjohn, S.C. Feil, W.J. McKinstry, R.K. Tweten, and M.W. Parker Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form Cell 89 1997 685 692 (Pubitemid 27516171)
    • (1997) Cell , vol.89 , Issue.5 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 197
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • DOI 10.1021/bi049002c
    • H. Zhao, E.K.J. Tuominen, and P.K.J. Kinnunen Formation of amyloid fibers triggered by phosphatidylserine-containing membranes Biochemistry 43 2004 10302 10307 (Pubitemid 39079303)
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 198
    • 0000181355 scopus 로고
    • A thermodynamic model of the lamellar to inverse hexagonal phase transition of lipid membrane-water systems
    • G.L. Kirk, S.M. Gruner, and D.L. Stein A thermodynamic model of the lamellar to inverse hexagonal phase transition of lipid membrane-water systems Biochemistry 23 1984 1093 1102
    • (1984) Biochemistry , vol.23 , pp. 1093-1102
    • Kirk, G.L.1    Gruner, S.M.2    Stein, D.L.3
  • 199
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • DOI 10.1016/S0304-4157(98)00015-X, PII S030441579800015X
    • R.M. Epand Lipid polymorphism and protein-lipid interactions Biochim Biophys Acta (BBA) - Rev Biomembr 1376 1998 353 368 (Pubitemid 28517885)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 353-368
    • Epand, R.M.1
  • 201
    • 0030780275 scopus 로고    scopus 로고
    • Biological significance of lipid polymorphism: The cubic phases
    • DOI 10.1016/S0959-440X(97)80075-9
    • V. Luzzati Biological significance of lipid polymorphism: the cubic phases Curr Opin Struct Biol 7 1997 661 668 (Pubitemid 27472585)
    • (1997) Current Opinion in Structural Biology , vol.7 , Issue.5 , pp. 661-668
    • Luzzati, V.1
  • 202
    • 0021104560 scopus 로고
    • Three-dimensional arrangement of the cell wall protein of Sulfolobus acidocaldarius
    • J.F. Deatherage, K.A. Taylor, L.A. Amos, and M.F. Moody Three-dimensional arrangement of the cell wall protein of Sulfolobus acidocaldarius J Mol Biol 167 1983 823 848
    • (1983) J Mol Biol , vol.167 , pp. 823-848
    • Deatherage, J.F.1    Taylor, K.A.2    Amos, L.A.3    Moody, M.F.4
  • 203
    • 0034462310 scopus 로고    scopus 로고
    • Modulation of membrane curvature by peptides
    • DOI 10.1002/1097-0282(2000)55:5<358::AID-BIP1009>3.0.CO;2-8
    • R.M. Epand, and R.F. Epand Modulation of membrane curvature by peptides Pept Sci 55 2000 358 363 (Pubitemid 32246521)
    • (2000) Biopolymers - Peptide Science Section , vol.55 , Issue.5 , pp. 358-363
    • Epand, R.M.1    Epand, R.F.2
  • 204
    • 77956713445 scopus 로고    scopus 로고
    • Chapter 6 modulation of lipid polymorphism by peptides
    • R.M. Epand, Academic Press, Inc.
    • R.M. Epand Chapter 6 modulation of lipid polymorphism by peptides R.M. Epand, Current topics in membranes and transport 1997 Academic Press, Inc. 237 252
    • (1997) Current Topics in Membranes and Transport , pp. 237-252
    • Epand, R.M.1
  • 205
    • 34948829603 scopus 로고    scopus 로고
    • How lipids influence the mode of action of membrane-active peptides
    • DOI 10.1016/j.bbamem.2007.06.015, PII S0005273607002295
    • E. Sevcsik, G. Pabst, A. Jilek, and K. Lohner How lipids influence the mode of action of membrane-active peptides Biochim Biophys Acta (BBA) - Biomembr 1768 2007 2586 2595 (Pubitemid 47532036)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.10 , pp. 2586-2595
    • Sevcsik, E.1    Pabst, G.2    Jilek, A.3    Lohner, K.4
  • 206
    • 28244489607 scopus 로고    scopus 로고
    • Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
    • DOI 10.1021/bi051302m
    • J.-P.S. Powers, A. Tan, A. Ramamoorthy, and R.E.W. Hancock Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes Biochemistry 44 2005 15504 15513 (Pubitemid 41706134)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15504-15513
    • Powers, J.-P.S.1    Tan, A.2    Ramamoorthy, A.3    Hancock, R.E.W.4
  • 207
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • E.J. Prenner, R.N.A.H. Lewis, and R.N. McElhaney The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes Biochim Biophys Acta (BBA) - Biomembr 1462 1999 201 221
    • (1999) Biochim Biophys Acta (BBA) - Biomembr , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 208
    • 0030853508 scopus 로고    scopus 로고
    • Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity
    • DOI 10.1021/bi962785k
    • E.J. Prenner, R.N.A.H. Lewis, K.C. Neuman, S.M. Gruner, L.H. Kondejewski, and R.S. Hodges Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity Biochemistry 36 1997 7906 7916 (Pubitemid 27287204)
    • (1997) Biochemistry , vol.36 , Issue.25 , pp. 7906-7916
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Neuman, K.C.3    Gruner, S.M.4    Kondejewski, L.H.5    Hodges, R.S.6    McElhaney, R.N.7
  • 209
    • 0025403162 scopus 로고
    • Cubic phases in surfactant and surfactant-like lipid systems
    • K. Fontell Cubic phases in surfactant and surfactant-like lipid systems Colloid Polym Sci 268 1990 264 285 (Pubitemid 20717835)
    • (1990) Colloid and Polymer Science , vol.268 , Issue.3 , pp. 264-285
    • Fontell, K.1
  • 210
  • 212
    • 0032929807 scopus 로고    scopus 로고
    • Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamines
    • DOI 10.1016/S0005-2736(99)00027-9, PII S0005273699000279
    • R. El Jastimi, and M. Lafleur Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamines Biochim Biophys Acta (BBA) - Biomembr 1418 1999 97 105 (Pubitemid 29182749)
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1418 , Issue.1 , pp. 97-105
    • El Jastimi, R.1    Lafleur, M.2
  • 213
    • 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
    • S.L. Keller, S.M. Gruner, and K. Gawrisch Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures Biochim Biophys Acta (BBA) - Biomembr 1278 1996 241 246 (Pubitemid 26062579)
    • (1996) Biochimica et Biophysica Acta - Biomembranes , vol.1278 , Issue.2 , pp. 241-246
    • Keller, S.L.1    Gruner, S.M.2    Gawrisch, K.3
  • 217
    • 0037416988 scopus 로고    scopus 로고
    • 2 by antimicrobial peptides
    • DOI 10.1128/AAC.47.3.965-971.2003
    • H. Zhao, and P.K.J. Kinnunen Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides Antimicrob Agents Chemother 47 2003 965 971 (Pubitemid 36254222)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.3 , pp. 965-971
    • Zhao, H.1    Kinnunen, P.K.J.2
  • 218
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • DOI 10.1006/bbrc.1998.8159
    • C.B. Park, H.S. Kim, and S.C. Kim Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions Biochem Biophys Res Commun 244 1998 253 257 (Pubitemid 28419934)
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.1 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 219
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • DOI 10.1073/pnas.150518097
    • C.B. Park, K.-S. Yi, K. Matsuzaki, M.S. Kim, and S.C. Kim Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II Proc Natl Acad Sci USA 97 2000 8245 8250 (Pubitemid 30639657)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.15 , pp. 8245-8250
    • Park, C.B.1    Yi, K.-S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 220
    • 0030032395 scopus 로고    scopus 로고
    • Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide
    • J. Shi, C. Ross, M. Chengappa, M. Sylte, D. McVey, and F. Blecha Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide Antimicrob Agents Chemother 40 1996 115 121 (Pubitemid 26020751)
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , Issue.1 , pp. 115-121
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Sylte, M.J.4    McVey, D.S.5    Blecha, F.6
  • 221
    • 77951224521 scopus 로고    scopus 로고
    • An antimicrobial peptide that targets DNA repair intermediates in vitro inhibits Salmonella growth within murine macrophages
    • L.Y. Su, D.L. Willner, and A.M. Segall An antimicrobial peptide that targets DNA repair intermediates in vitro inhibits Salmonella growth within murine macrophages Antimicrob Agents Chemother 54 2010 1888 1899
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1888-1899
    • Su, L.Y.1    Willner, D.L.2    Segall, A.M.3
  • 222
    • 0041816347 scopus 로고    scopus 로고
    • The action of the bacterial toxin microcin B17
    • O.A. Pierrat, and A. Maxwell The action of the bacterial toxin microcin B17 J Biol Chem 278 2003 35016 35023
    • (2003) J Biol Chem , vol.278 , pp. 35016-35023
    • Pierrat, O.A.1    Maxwell, A.2
  • 223
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli
    • DOI 10.1128/AAC.46.3.605-614.2002
    • A. Patrzykat, C.L. Friedrich, L. Zhang, V. Mendoza, and R.E.W. Hancock Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli Antimicrob Agents Chemother 46 2002 605 614 (Pubitemid 34162506)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.3 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.W.5
  • 225
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • DOI 10.1021/bi002656a
    • G. Kragol, S. Lovas, G. Varadi, B.A. Condie, R. Hoffmann, and L. Otvos The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding Biochemistry 40 2001 3016 3026 (Pubitemid 32206189)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos Jr., L.6
  • 227
    • 34250883860 scopus 로고    scopus 로고
    • Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria
    • DOI 10.1016/j.yexcr.2007.05.015, PII S0014482707002388
    • J.S. Mader, A. Richardson, J. Salsman, D. Top, R. de Antueno, and R. Duncan Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria Exp Cell Res 313 2007 2634 2650 (Pubitemid 46977347)
    • (2007) Experimental Cell Research , vol.313 , Issue.12 , pp. 2634-2650
    • Mader, J.S.1    Richardson, A.2    Salsman, J.3    Top, D.4    De Antueno, R.5    Duncan, R.6    Hoskin, D.W.7
  • 228
    • 25444520813 scopus 로고    scopus 로고
    • Alterations in membrane fluidity, lipid metabolism, mitochondrial activity, and lipophosphoglycan expression in pentamidine-resistant Leishmania
    • DOI 10.1007/s004360050361
    • M. Basselin, and M. Robert-Gero Alterations in membrane fluidity, lipid metabolism, mitochondrial activity, and lipophosphoglycan expression in pentamidine-resistant Leishmania Parasitol Res 84 1998 78 83 (Pubitemid 28097631)
    • (1998) Parasitology Research , vol.84 , Issue.1 , pp. 78-83
    • Basselin, M.1    Robert-Gero, M.2
  • 229
    • 0017744251 scopus 로고
    • Induction of polymyxin resistance in Pseudomonas fluorescens by phosphate limitation
    • E. Dorrer, and M. Teuber Induction of polymyxin resistance in Pseudomonas fluorescens by phosphate limitation Arch Microbiol 114 1977 87 89 (Pubitemid 8148392)
    • (1977) Archives of Microbiology , vol.114 , Issue.1 , pp. 87-89
    • Dorrer, E.1    Teuber, M.2
  • 231
    • 0036192372 scopus 로고    scopus 로고
    • Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes
    • DOI 10.1046/j.1365-2958.2002.02723.x
    • E. Abachin, C. Poyart, E. Pellegrini, E. Milohanic, F. Fiedler, and P. Berche Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes Mol Microbiol 43 2002 1 14 (Pubitemid 34212186)
    • (2002) Molecular Microbiology , vol.43 , Issue.1 , pp. 1-14
    • Abachin, E.1    Poyart, C.2    Pellegrini, E.3    Milohanic, E.4    Fiedler, F.5    Berche, P.6    Trieu-Cuot, P.7
  • 232
    • 0141789720 scopus 로고    scopus 로고
    • Attenuated virulence of Streptococcus agalactiae deficient in D-alanyl-lipoteichoic acid is due to an increased susceptibility to defensins and phagocytic cells
    • DOI 10.1046/j.1365-2958.2003.03655.x
    • C. Poyart, E. Pellegrini, M. Marceau, M. Baptista, F. Jaubert, and M.-C. Lamy Attenuated virulence of Streptococcus agalactiae deficient in D-alanyl-lipoteichoic acid is due to an increased susceptibility to defensins and phagocytic cells Mol Microbiol 49 2003 1615 1625 (Pubitemid 37153520)
    • (2003) Molecular Microbiology , vol.49 , Issue.6 , pp. 1615-1625
    • Poyart, C.1    Pellegrini, E.2    Marceau, M.3    Baptista, M.4    Jaubert, F.5    Lamy, M.-C.6    Trieu-Cuot, P.7
  • 234
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: Role in resistance to host innate immunity
    • DOI 10.1016/S1286-4579(01)01494-0
    • R.K. Ernst, T. Guina, and S.I. Miller Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity Microb Infect 3 2001 1327 1334 (Pubitemid 34033769)
    • (2001) Microbes and Infection , vol.3 , Issue.14-15 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 235
    • 0033976515 scopus 로고    scopus 로고
    • Bacterial phosphorylcholine decreases susceptibility to the antimicrobial peptide LL-37/hCAP18 expressed in the upper respiratory tract
    • DOI 10.1128/IAI.68.3.1664-1671.2000
    • E.S. Lysenko, J. Gould, R. Bals, J.M. Wilson, and J.N. Weiser Bacterial phosphorylcholine decreases susceptibility to the antimicrobial peptide LL-37/hCAP18 expressed in the upper respiratory tract Infect Immun 68 2000 1664 1671 (Pubitemid 30108570)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1664-1671
    • Lysenko, E.S.1    Gould, J.2    Bals, R.3    Wilson, J.M.4    Weiser, J.N.5
  • 236
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides
    • DOI 10.1111/j.1749-6632.1996.tb52963.x
    • R.I. Lehrer, and T. Ganz Endogenous vertebrate antibiotics: defensins, protegrins, and other cysteine-rich antimicrobial peptides Ann NY Acad Sci 797 1996 228 239 (Pubitemid 27055594)
    • (1996) Annals of the New York Academy of Sciences , vol.797 , pp. 228-239
    • Lehrer, R.I.1    Ganz, T.2
  • 237
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • M.R. Yeaman, A.S. Bayer, S.P. Koo, W. Foss, and P.M. Sullam Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action J Clin Invest 101 1998 178 187 (Pubitemid 28058917)
    • (1998) Journal of Clinical Investigation , vol.101 , Issue.1 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.-P.3    Foss, W.4    Sullam, P.M.5
  • 238
    • 0019776488 scopus 로고
    • Dipoles of the α-helix and β-sheet: Their role in protein folding
    • W.G.J. Hol, L.M. Halie, and C. Sander Dipoles of the [alpha]-helix and [beta]-sheet: their role in protein folding Nature 294 1981 532 536 (Pubitemid 12164574)
    • (1981) Nature , vol.294 , Issue.5841 , pp. 532-536
    • Hol, W.G.J.1    Halie, L.M.2    Sander, C.3
  • 239
    • 0033977173 scopus 로고    scopus 로고
    • Candida albicans mutants deficient in respiration are resistant to the small cationic salivary antimicrobial peptide histatin 5
    • DOI 10.1128/AAC.44.2.348-354.2000
    • C. Gyurko, U. Lendenmann, R.F. Troxler, and F.G. Oppenheim Candida albicans mutants deficient in respiration are resistant to the small cationic salivary antimicrobial peptide histatin 5 Antimicrob Agents Chemother 44 2000 348 354 (Pubitemid 30060730)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.2 , pp. 348-354
    • Gyurko, C.1    Lendenmann, U.2    Troxler, R.F.3    Oppenheim, F.G.4
  • 240
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A
    • DOI 10.1128/AAC.47.1.1-6.2003
    • R.W. Hong, M. Shchepetov, J.N. Weiser, and P.H. Axelsen Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A Antimicrob Agents Chemother 47 2003 1 6 (Pubitemid 36070334)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.1 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 242
    • 72249091894 scopus 로고    scopus 로고
    • A protein important for antimicrobial peptide resistance, YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC
    • M.C. Pilonieta, K.D. Erickson, R.K. Ernst, and C.S. Detweiler A protein important for antimicrobial peptide resistance, YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpC J Bacteriol 191 2009 7243 7252
    • (2009) J Bacteriol , vol.191 , pp. 7243-7252
    • Pilonieta, M.C.1    Erickson, K.D.2    Ernst, R.K.3    Detweiler, C.S.4
  • 243
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • DOI 10.1128/JB.182.14.4077-4086.2000
    • T. Guina, E.C. Yi, H. Wang, M. Hackett, and S.I. Miller A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to [alpha]-helical antimicrobial peptides J Bacteriol 182 2000 4077 4086 (Pubitemid 30436571)
    • (2000) Journal of Bacteriology , vol.182 , Issue.14 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 244
    • 34247182998 scopus 로고    scopus 로고
    • The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5
    • DOI 10.1016/j.febslet.2007.03.049, PII S0014579307003213
    • P. Ramu, R. Tanskanen, M. Holmberg, K. Lähteenmäki, T.K. Korhonen, and S. Meri The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5 FEBS Lett 581 2007 1716 1720 (Pubitemid 46604815)
    • (2007) FEBS Letters , vol.581 , Issue.9 , pp. 1716-1720
    • Ramu, P.1    Tanskanen, R.2    Holmberg, M.3    Lahteenmaki, K.4    Korhonen, T.K.5    Meri, S.6
  • 245
    • 0036796983 scopus 로고    scopus 로고
    • Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B
    • H. Ulvatne, H.H. Haukland, O. Samuelsen, M. Kramer, and L.H. Vorland Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B J Antimicrob Chemother 50 2002 461 467 (Pubitemid 35214784)
    • (2002) Journal of Antimicrobial Chemotherapy , vol.50 , Issue.4 , pp. 461-467
    • Ulvatne, H.1    Haukland, H.H.2    Samuelsen, O.3    Kramer, M.4    Vorland, L.H.5
  • 246
    • 0034697120 scopus 로고    scopus 로고
    • Formation and characterization of a single Trp-Trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity
    • DOI 10.1074/jbc.275.16.12017
    • K. Ösapay, D. Tran, A.S. Ladokhin, S.H. White, A.H. Henschen, and M.E. Selsted Formation and characterization of a single Trp-Trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity J Biol Chem 275 2000 12017 12022 (Pubitemid 30237775)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 12017-12022
    • Osapay, K.1    Tran, D.2    Ladokhin, A.S.3    White, S.H.4    Henschen, A.H.5    Selsted, M.E.6
  • 247
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • DOI 10.1073/pnas.95.4.1829
    • W.M. Shafer, X.-D. Qu, A.J. Waring, and R.I. Lehrer Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family Proc Natl Acad Sci USA 95 1998 1829 1833 (Pubitemid 28103479)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.4 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.-D.2    Waring, A.J.3    Lehrer, R.I.4
  • 248
    • 0033925707 scopus 로고    scopus 로고
    • Temperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia
    • DOI 10.1046/j.1365-2958.2000.01956.x
    • J.A. Bengoechea, and M. Skurnik Temperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia Mol Microbiol 37 2000 67 80 (Pubitemid 30479358)
    • (2000) Molecular Microbiology , vol.37 , Issue.1 , pp. 67-80
    • Bengoechea, J.A.1    Skurnik, M.2
  • 249
    • 0032862511 scopus 로고    scopus 로고
    • Plasmid-mediated resistance to thrombin-induced platelet microbicidal protein in staphylococci: Role of the qacA locus
    • L.I. Kupferwasser, R.A. Skurray, M.H. Brown, N. Firth, M.R. Yeaman, and A.S. Bayer Plasmid-mediated resistance to thrombin-induced platelet microbicidal protein in staphylococci: role of the qacA locus Antimicrob Agents Chemother 43 1999 2395 2399 (Pubitemid 29471216)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.10 , pp. 2395-2399
    • Kupferwasser, L.I.1    Skurray, R.A.2    Brown, M.H.3    Firth, N.4    Yeaman, M.R.5    Bayer, A.S.6
  • 250
    • 48849102268 scopus 로고    scopus 로고
    • Vibrio cholerae RND family efflux systems are required for antimicrobial resistance, optimal virulence factor production, and colonization of the infant mouse small intestine
    • X.R. Bina, D. Provenzano, N. Nguyen, and J.E. Bina Vibrio cholerae RND family efflux systems are required for antimicrobial resistance, optimal virulence factor production, and colonization of the infant mouse small intestine Infect Immun 76 2008 3595 3605
    • (2008) Infect Immun , vol.76 , pp. 3595-3605
    • Bina, X.R.1    Provenzano, D.2    Nguyen, N.3    Bina, J.E.4
  • 252
  • 253
    • 0346729747 scopus 로고    scopus 로고
    • 2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii
    • DOI 10.1016/j.peptides.2003.08.003
    • A. Giacometti, O. Cirioni, W. Kamysz, G. D'Amato, C. Silvestri, and M.S. Del Prete Comparative activities of cecropin A, melittin, and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii Peptides 24 2003 1315 1318 (Pubitemid 38045538)
    • (2003) Peptides , vol.24 , Issue.9 , pp. 1315-1318
    • Giacometti, A.1    Cirioni, O.2    Kamysz, W.3    D'Amato, G.4    Silvestri, C.5    Del Prete, M.S.6    Lukasiak, J.7    Scalise, G.8
  • 254
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • DOI 10.1007/s00018-005-4560-2
    • N. Papo, and Y. Shai Host defense peptides as new weapons in cancer treatment Cell Mol Life Sci 62 2005 784 790 (Pubitemid 40655628)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.7-8 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 255
    • 70350708570 scopus 로고    scopus 로고
    • Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1-11)
    • W. van der Velden, T. van Iersel, N. Blijlevens, and J.P. Donnelly Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1-11) BMC Med 7 2009 44
    • (2009) BMC Med , vol.7 , pp. 44
    • Van Der Velden, W.1    Van Iersel, T.2    Blijlevens, N.3    Donnelly, J.P.4
  • 256
    • 0034675328 scopus 로고    scopus 로고
    • Recombinant bactericidal/permeability-increasing protein (rBPI21) as adjunctive treatment for children with severe meningococcal sepsis: A randomised trial
    • M. Levin, P.A. Quint, B. Goldstein, P. Barton, J.S. Bradley, and S.D. Shemie Recombinant bactericidal/permeability-increasing protein (rBPI21) as adjunctive treatment for children with severe meningococcal sepsis: a randomised trial Lancet 356 2000 961 967
    • (2000) Lancet , vol.356 , pp. 961-967
    • Levin, M.1    Quint, P.A.2    Goldstein, B.3    Barton, P.4    Bradley, J.S.5    Shemie, S.D.6
  • 257
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • H.D. Herce, and A.E. Garcia Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes Proc Natl Acad Sci 104 2007 20805 20810
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 258
    • 77954215748 scopus 로고    scopus 로고
    • The multiple faces of self-assembled lipidic systems
    • G. Tresset The multiple faces of self-assembled lipidic systems PMC Biophys 2 2009 3
    • (2009) PMC Biophys , vol.2 , pp. 3
    • Tresset, G.1
  • 259
    • 0014730125 scopus 로고
    • A novel cubic phase-A cage-like network of rods with enclosed spherical micelles
    • A. Tardieu, and V. Luzzati A novel cubic phase-A cage-like network of rods with enclosed spherical micelles Biochim Biophys Acta (BBA) - Biomembr 219 1970 11 17
    • (1970) Biochim Biophys Acta (BBA) - Biomembr , vol.219 , pp. 11-17
    • Tardieu, A.1    Luzzati, V.2
  • 260
    • 84960621095 scopus 로고
    • On the structure of the cubic phase I, in some lipid-water systems
    • K. Fontell, K.K. Fox, and E. Hansson On the structure of the cubic phase I, in some lipid-water systems Mol Cryst Liquid Cryst Lett 1 1985 9 17
    • (1985) Mol Cryst Liquid Cryst Lett , vol.1 , pp. 9-17
    • Fontell, K.1    Fox, K.K.2    Hansson, E.3
  • 261
    • 0023979182 scopus 로고
    • Periodic systems of frustrated fluid films and 'micellar' cubic structures in liquid crystals
    • J. Charvolin, and J.F. Sadoc Periodic systems of frustrated fluid films and «micellar» cubic structures in liquid crystals J Phys France 49 1988 521 526 (Pubitemid 18593116)
    • (1988) Journal de physique Paris , vol.49 , Issue.3 , pp. 521-526
    • Charvolin, J.1    Sadoc, J.F.2
  • 263
    • 0029975929 scopus 로고    scopus 로고
    • Wild-type Escherichia coli cells regulate the membrane lipid composition in a window between gel and non-lamellar structures
    • S. Morein, A.-S. Andersson, L. Rilfors, and G. Lindblom Wild-type Escherichia coli cells regulate the membrane lipid composition in a window between gel and non-lamellar structures J Biol Chem 271 1996 6801 6809
    • (1996) J Biol Chem , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.-S.2    Rilfors, L.3    Lindblom, G.4
  • 264
    • 0015821003 scopus 로고
    • The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
    • A.J. Verkleij, R.F.A. Zwaal, B. Roelofsen, P. Comfurius, D. Kastelijn, and L.L.M. van Deenen The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy Biochim Biophys Acta (BBA) - Biomembr 323 1973 178 193
    • (1973) Biochim Biophys Acta (BBA) - Biomembr , vol.323 , pp. 178-193
    • Verkleij, A.J.1    Zwaal, R.F.A.2    Roelofsen, B.3    Comfurius, P.4    Kastelijn, D.5    Van Deenen, L.L.M.6
  • 265
    • 0028244076 scopus 로고
    • Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus
    • DOI 10.1007/BF00277157
    • W. Fischer Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus Med Microbiol Immunol 183 1994 61 76 (Pubitemid 24210541)
    • (1994) Medical Microbiology and Immunology , vol.183 , Issue.2 , pp. 61-76
    • Fischer, W.1
  • 266
    • 0026550672 scopus 로고
    • Binding of tachyplesin i to DNA revealed by footprinting analysis: Significant contribution of secondary structure to DNA binding and implication for biological action
    • A. Yonezawa, J. Kuwahara, N. Fujii, and Y. Sugiura Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action Biochemistry 31 1992 2998 3004
    • (1992) Biochemistry , vol.31 , pp. 2998-3004
    • Yonezawa, A.1    Kuwahara, J.2    Fujii, N.3    Sugiura, Y.4
  • 267
    • 54849411014 scopus 로고    scopus 로고
    • Antifungal mechanism of antibacterial peptide, ABP-CM4, from Bombyx mori against Aspergillus niger
    • J. Zhang, X. Wu, and S.-Q. Zhang Antifungal mechanism of antibacterial peptide, ABP-CM4, from Bombyx mori against Aspergillus niger Biotechnol Lett 30 2008 2157 2163
    • (2008) Biotechnol Lett , vol.30 , pp. 2157-2163
    • Zhang, J.1    Wu, X.2    Zhang, S.-Q.3
  • 270
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • H.G. Boman, B. Agerberth, and A. Boman Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine Infect Immun 61 1993 2978 2984 (Pubitemid 23182296)
    • (1993) Infection and Immunity , vol.61 , Issue.7 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 271
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • DOI 10.1016/S0378-1097(98)00008-1, PII S0378109798000081
    • C. Subbalakshmi, and N. Sitaram Mechanism of antimicrobial action of indolicidin FEMS Microbiol Lett 160 1998 91 96 (Pubitemid 28098557)
    • (1998) FEMS Microbiology Letters , vol.160 , Issue.1 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 273
    • 0026526445 scopus 로고
    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
    • R.A. Salomon, and R.N. Farias Microcin 25, a novel antimicrobial peptide produced by Escherichia coli J Bacteriol 174 1992 7428 7435
    • (1992) J Bacteriol , vol.174 , pp. 7428-7435
    • Salomon, R.A.1    Farias, R.N.2
  • 274
    • 0001015635 scopus 로고
    • Reduction of purothionin by the wheat seed thioredoxin system
    • T.C. Johnson, K. Wada, B.B. Buchanan, and A. Holmgren Reduction of purothionin by the wheat seed thioredoxin system Plant Physiol 85 1987 446 451
    • (1987) Plant Physiol , vol.85 , pp. 446-451
    • Johnson, T.C.1    Wada, K.2    Buchanan, B.B.3    Holmgren, A.4
  • 275
    • 67349282270 scopus 로고    scopus 로고
    • The proline-rich antibacterial peptide Bac7 binds to and inhibits in vitro the molecular chaperone DnaK
    • M. Scocchi, C. Lüthy, P. Decarli, G. Mignogna, P. Christen, and R. Gennaro The proline-rich antibacterial peptide Bac7 binds to and inhibits in vitro the molecular chaperone DnaK Int J Pept Res Ther 15 2009 147 155
    • (2009) Int J Pept Res Ther , vol.15 , pp. 147-155
    • Scocchi, M.1    Lüthy, C.2    Decarli, P.3    Mignogna, G.4    Christen, P.5    Gennaro, R.6
  • 276
    • 77952976637 scopus 로고    scopus 로고
    • Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II
    • T. Schneider, T. Kruse, R. Wimmer, I. Wiedemann, V. Sass, and U. Pag Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II Science 328 2010 1168 1172
    • (2010) Science , vol.328 , pp. 1168-1172
    • Schneider, T.1    Kruse, T.2    Wimmer, R.3    Wiedemann, I.4    Sass, V.5    Pag, U.6
  • 278
    • 0033841237 scopus 로고    scopus 로고
    • Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crunstacea, Decapoda)
    • D. Destoumieux, M. Munoz, P. Bulet, and E. Bachre Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda) Cell Mol Life Sci 57 2000 1260 1271 (Pubitemid 30663482)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.8-9 , pp. 1260-1271
    • Destoumieux, D.1    Munoz, M.2    Bulet, P.3    Bachere, E.4
  • 280
    • 60849108318 scopus 로고    scopus 로고
    • Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death
    • M. Delgado, P. Anderson, J.A. Garcia-Salcedo, M. Caro, and E. Gonzalez-Rey Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death Cell Death Differ 16 2008 406 416
    • (2008) Cell Death Differ , vol.16 , pp. 406-416
    • Delgado, M.1    Anderson, P.2    Garcia-Salcedo, J.A.3    Caro, M.4    Gonzalez-Rey, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.