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Volumn 1838, Issue 11, 2014, Pages 2899-2909

Elucidation of mechanisms of interaction of a multifunctional peptide Pa-MAP with lipid membranes

Author keywords

Antimicrobial; Electrical impedance spectroscopy; Membrane; Multifunctional peptide; Pleuronectes americanus

Indexed keywords

AMINO ACID; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; LIPID; PEPTIDE; PLEURONECTES AMERICANUS PEPTIDE MAP; UNCLASSIFIED DRUG;

EID: 84906039688     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.08.002     Document Type: Article
Times cited : (9)

References (67)
  • 1
    • 62949152118 scopus 로고    scopus 로고
    • Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water
    • S.M. Mandal, S. Dey, M. Mandal, S. Sarkar, S. Maria-Neto, and O.L. Franco Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water Peptides 30 2009 633 637
    • (2009) Peptides , vol.30 , pp. 633-637
    • Mandal, S.M.1    Dey, S.2    Mandal, M.3    Sarkar, S.4    Maria-Neto, S.5    Franco, O.L.6
  • 2
    • 67649255997 scopus 로고    scopus 로고
    • Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR
    • E. Strandberg, P. Tremouilhac, P. Wadhwani, and A.S. Ulrich Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR Biochim. Biophys. Acta 1788 2009 1667 1679
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1667-1679
    • Strandberg, E.1    Tremouilhac, P.2    Wadhwani, P.3    Ulrich, A.S.4
  • 3
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • R.E. Hancock, and H.G. Sahl Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 24 2006 1551 1557 (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 4
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • L.J. Zhang, A. Rozek, and R.E.W. Hancock Interaction of cationic antimicrobial peptides with model membranes J. Biol. Chem. 276 2001 35714 35722
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.J.1    Rozek, A.2    Hancock, R.E.W.3
  • 5
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • L.T. Nguyen, E.F. Haney, and H.J. Vogel The expanding scope of antimicrobial peptide structures and their modes of action Trends Biotechnol. 29 2011 464 472
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 6
    • 0002336563 scopus 로고    scopus 로고
    • The role of membrane lipid composition in cell targeting of antimicrobial peptides
    • K. Lohner, Horizon Scientific Press
    • K. Lohner The role of membrane lipid composition in cell targeting of antimicrobial peptides K. Lohner, Development of Novel Antimicrobial Agents: Emerging Strategies 2001 Horizon Scientific Press 149 165
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1
  • 7
    • 0036188648 scopus 로고    scopus 로고
    • Rational design of α-helical antifreeze peptides
    • DOI 10.1046/j.1397-002x.2001.00001.x
    • M.J. Kuiper, J.V. Fecondo, and M.G. Wong Rational design of alpha-helical antifreeze peptides J. Pept. Res. 59 2002 1 8 (Pubitemid 34185255)
    • (2002) Journal of Peptide Research , vol.59 , Issue.1 , pp. 1-8
    • Kuiper, M.J.1    Fecondo, J.V.2    Wong, M.G.3
  • 8
    • 0030049438 scopus 로고    scopus 로고
    • Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences
    • DOI 10.1074/jbc.271.8.4106
    • Z. Gong, K.V. Ewart, Z. Hu, G.L. Fletcher, and C.L. Hew Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences J. Biol. Chem. 271 1996 4106 4112 (Pubitemid 26070507)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4106-4112
    • Gong, Z.1    Ewart, K.V.2    Hu, Z.3    Fletcher, G.L.4    Hew, C.L.5
  • 9
    • 84877266191 scopus 로고    scopus 로고
    • In vivo antimicrobial evaluation of an alanine-rich peptide derived from Pleuronectes americanus
    • L.D. Teixeira, O.N. Silva, L. Migliolo, I.C.M. Fensterseifer, and O.L. Franco In vivo antimicrobial evaluation of an alanine-rich peptide derived from Pleuronectes americanus Peptides 42 2013 144 148
    • (2013) Peptides , vol.42 , pp. 144-148
    • Teixeira, L.D.1    Silva, O.N.2    Migliolo, L.3    Fensterseifer, I.C.M.4    Franco, O.L.5
  • 10
    • 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
  • 11
    • 13844308071 scopus 로고    scopus 로고
    • Membrane interactions of host-defense peptides studied in model systems
    • DOI 10.2174/1389203053027511
    • R. Jelinek, and S. Kolusheva Membrane interactions of host-defense peptides studied in model systems Curr. Protein Pept. Sci. 6 2005 103 114 (Pubitemid 40259805)
    • (2005) Current Protein and Peptide Science , vol.6 , Issue.1 , pp. 103-114
    • Jelinek, R.1    Kolusheva, S.2
  • 12
    • 0000552736 scopus 로고
    • Spontaneous assembly of bilayer-membranes on a solid-surface
    • T. Martynski, and H.T. Tien Spontaneous assembly of bilayer-membranes on a solid-surface Bioelectrochem. Bioenerg. 25 1991 317 324
    • (1991) Bioelectrochem. Bioenerg. , vol.25 , pp. 317-324
    • Martynski, T.1    Tien, H.T.2
  • 13
    • 0032313368 scopus 로고    scopus 로고
    • Supported planar lipid bilayers (s-BLMs) as electrochemical biosensors
    • PII S0013468698001078
    • H.T. Tien, and A.L. Ottova Supported planar lipid bilayers (s-BLM) as electrochemical biosensors Electrochim. Acta 43 1998 3587 3610 (Pubitemid 128412595)
    • (1998) Electrochimica Acta , vol.43 , Issue.23 , pp. 3587-3610
    • Tien, H.T.1    Ottova, A.L.2
  • 14
    • 0032367779 scopus 로고    scopus 로고
    • Supported bilayer lipid membranes as ion and molecular probes
    • H.T. Tien, R.H. Barish, L.Q. Gu, and A.L. Ottova Supported bilayer lipid membranes as ion and molecular probes Anal. Sci. 14 1998 3 18
    • (1998) Anal. Sci. , vol.14 , pp. 3-18
    • Tien, H.T.1    Barish, R.H.2    Gu, L.Q.3    Ottova, A.L.4
  • 15
    • 84859621556 scopus 로고    scopus 로고
    • Interactions of membrane active peptides with planar supported bilayers: An impedance spectroscopy study
    • J. Lin, J. Motylinski, A.J. Krauson, W.C. Wimley, P.C. Searson, and K. Hristova Interactions of membrane active peptides with planar supported bilayers: an impedance spectroscopy study Langmuir 28 2012 6088 6096
    • (2012) Langmuir , vol.28 , pp. 6088-6096
    • Lin, J.1    Motylinski, J.2    Krauson, A.J.3    Wimley, W.C.4    Searson, P.C.5    Hristova, K.6
  • 16
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • DOI 10.1016/S0005-2736(01)00382-0, PII S0005273601003820
    • A.S. Ladokhin, and S.H. White 'Detergent-like' permeabilization of anionic lipid vesicles by melittin Biochim. Biophys. Acta 1514 2001 253 260 (Pubitemid 32831013)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1514 , Issue.2 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 17
    • 84888247576 scopus 로고    scopus 로고
    • Mechanistic aspects of peptide-membrane interactions determined by optical, dielectric and piezoelectric techniques: An overview
    • M.D.L. Oliveira, O.L. Franco, J.M. Nascimento, C.P. de Melo, and C.A.S. Andrade Mechanistic aspects of peptide-membrane interactions determined by optical, dielectric and piezoelectric techniques: an overview Curr. Protein Pept. Sci. 14 2013 543 555
    • (2013) Curr. Protein Pept. Sci. , vol.14 , pp. 543-555
    • Oliveira, M.D.L.1    Franco, O.L.2    Nascimento, J.M.3    De Melo, C.P.4    Andrade, C.A.S.5
  • 18
    • 52049088052 scopus 로고    scopus 로고
    • Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy
    • W.K. Chang, W.C. Wimley, P.C. Searson, K. Hristova, and M. Merzlyakov Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy Biochim. Biophys. Acta 1778 2008 2430 2436
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2430-2436
    • Chang, W.K.1    Wimley, W.C.2    Searson, P.C.3    Hristova, K.4    Merzlyakov, M.5
  • 19
    • 84861970313 scopus 로고    scopus 로고
    • Evaluation of magainin i interactions with lipid membranes: An optical and electrochemical study
    • J.M. Nascimento, O.L. Franco, M.D.L. Oliveira, and C.A.S. Andrade Evaluation of magainin I interactions with lipid membranes: an optical and electrochemical study Chem. Phys. Lipids 165 2012 537 544
    • (2012) Chem. Phys. Lipids , vol.165 , pp. 537-544
    • Nascimento, J.M.1    Franco, O.L.2    Oliveira, M.D.L.3    Andrade, C.A.S.4
  • 20
    • 0024910316 scopus 로고
    • Formation of self-assembled lipid bilayers on solid substrates
    • DOI 10.1016/0302-4598(89)87040-0
    • H.T. Tien, and Z. Salamon Formation of self-assembled lipid bilayers on solid substrates Bioelectrochem. Bioenerg. 22 1989 211 218 (Pubitemid 20116542)
    • (1989) Bioelectrochemistry and Bioenergetics , vol.22 , Issue.3 , pp. 211-218
    • Tien, H.T.1    Salamon, Z.2
  • 21
    • 0030106399 scopus 로고    scopus 로고
    • An agarose-stabilized BLM: A new method for forming bilayer lipid membranes
    • DOI 10.1016/0928-4931(95)00127-1
    • H.P. Yuan, A. Leitmannova-Ottova, and H.T. Tien An agarose-stabilized BLM: a new method for forming bilayer lipid membranes Mater. Sci. Eng. C 4 1996 35 38 (Pubitemid 126403191)
    • (1996) Materials Science and Engineering C , vol.4 , Issue.1 , pp. 35-38
    • Yuan, H.1    Leitmannova-Ottova, A.2    Tien, H.T.3
  • 22
    • 0345764882 scopus 로고    scopus 로고
    • Conductivity fluctuations in bilayer lipid membranes, formed on the support
    • V.I. Pasechnik, S.A. Ivanov, T. Hianik, M. Shnejdarkova, and B. Sivak Conductivity fluctuations in bilayer lipid membranes, formed on the support Biofizika 43 1998 61 68
    • (1998) Biofizika , vol.43 , pp. 61-68
    • Pasechnik, V.I.1    Ivanov, S.A.2    Hianik, T.3    Shnejdarkova, M.4    Sivak, B.5
  • 23
    • 0031032253 scopus 로고    scopus 로고
    • Stability of bilayer lipid membranes on different metallic supports
    • DOI 10.1016/S0956-5663(97)87060-1
    • M. Snejdarkova, M. Rehak, and M. Otto Stability of bilayer lipid membranes on different metallic supports Biosens. Bioelectron. 12 1997 145 153 (Pubitemid 27019743)
    • (1997) Biosensors and Bioelectronics , vol.12 , Issue.2 , pp. 145-153
    • Snejdarkova, M.1    Rehak, M.2    Otto, M.3
  • 25
    • 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 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
  • 26
    • 0021990499 scopus 로고
    • Toxicity determined in vitro by morphological alterations and neutral red absorption
    • DOI 10.1016/0378-4274(85)90046-3
    • E. Borenfreund, and J.A. Puerner Toxicity determined in vitro by morphological alterations and neutral red absorption Toxicol. Lett. 24 1985 119 124 (Pubitemid 15103513)
    • (1985) Toxicology Letters , vol.24 , Issue.2-3 , pp. 119-124
    • Borenfreund, E.1    Puerner, J.A.2
  • 27
    • 0001671557 scopus 로고
    • Note on the spectrophotometric determination of proteins in dilute solutions
    • J. Murphy, and M. Kies Note on the spectrophotometric determination of proteins in dilute solutions Biochim. Biophys. Acta 3 1960 382 384
    • (1960) Biochim. Biophys. Acta , vol.3 , pp. 382-384
    • Murphy, J.1    Kies, M.2
  • 28
    • 0033833996 scopus 로고    scopus 로고
    • Electrochemical biosensor based on supported planar lipid bilayers for fast detection of pathogenic bacteria
    • D. Ivnitski, E. Wilkins, H.T. Tien, and A. Ottova Electrochemical biosensor based on supported planar lipid bilayers for fast detection of pathogenic bacteria Electrochem. Commun. 2 2000 457 460
    • (2000) Electrochem. Commun. , vol.2 , pp. 457-460
    • Ivnitski, D.1    Wilkins, E.2    Tien, H.T.3    Ottova, A.4
  • 29
    • 38649122073 scopus 로고    scopus 로고
    • Electrical impedance spectroscopy investigation of surfactant-magnetite- polypyrrole particles
    • H.P. de Oliveira, C.A.S. Andrade, and C.P. de Melo Electrical impedance spectroscopy investigation of surfactant-magnetite-polypyrrole particles J. Colloid Interface Sci. 319 2008 441 449
    • (2008) J. Colloid Interface Sci. , vol.319 , pp. 441-449
    • De Oliveira, H.P.1    Andrade, C.A.S.2    De Melo, C.P.3
  • 32
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • M. Wiederstein, and M.J. Sippl ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins Nucleic Acids Res. 35 2007 W407 W410
    • (2007) Nucleic Acids Res. , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 35
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • T.J. Dolinsky, J.E. Nielsen, J.A. McCammon, and N.A. Baker PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 32 2004 W665 W667
    • (2004) Nucleic Acids Res. , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 37
    • 0031880829 scopus 로고    scopus 로고
    • Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations
    • S.J. Marrink, O. Berger, D.P. Tieleman, and F. Jaehnig Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations Biophys. J. 74 1998 931 943 (Pubitemid 28345286)
    • (1998) Biophysical Journal , vol.74 , pp. 931-943
    • Marrink, S.-J.1    Berger, O.2    Tieleman, P.3    Jahnig, F.4
  • 38
    • 84858795099 scopus 로고    scopus 로고
    • Computational design of peptide inhibitor based on modifications of proregion from Plutella xylostella midgut trypsin
    • J. Jitonnom, K. Lomthaisong, and V.S. Lee Computational design of peptide inhibitor based on modifications of proregion from Plutella xylostella midgut trypsin Chem. Biol. Drug Des. 79 2012 583 593
    • (2012) Chem. Biol. Drug Des. , vol.79 , pp. 583-593
    • Jitonnom, J.1    Lomthaisong, K.2    Lee, V.S.3
  • 40
    • 24144461618 scopus 로고    scopus 로고
    • Direct visualization of membrane leakage induced by the antibiotic peptides: Maculatin, citropin, and aurein
    • DOI 10.1529/biophysj.105.066589
    • E.E. Ambroggio, F. Separovic, J.H. Bowie, G.D. Fidelio, and L.A. Bagatolli Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein Biophys. J. 89 2005 1874 1881 (Pubitemid 41233542)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1874-1881
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.H.3    Fidelio, G.D.4    Bagatolli, L.A.5
  • 41
    • 77949517357 scopus 로고    scopus 로고
    • RBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes
    • M.M. Domingues, M.A.R.B. Castanho, and N.C. Santos rBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes Plos One 4 2009
    • (2009) Plos One , vol.4
    • Domingues, M.M.1    Castanho, M.A.R.B.2    Santos, N.C.3
  • 42
    • 0028765518 scopus 로고
    • A study of stability of supported liquid membranes by impedance spectroscopy
    • F.F. Zha, H.G.L. Coster, and A.G. Fane A study of stability of supported liquid membranes by impedance spectroscopy J. Membr. Sci. 93 1994 255 271
    • (1994) J. Membr. Sci. , vol.93 , pp. 255-271
    • Zha, F.F.1    Coster, H.G.L.2    Fane, A.G.3
  • 43
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols - Model ion channels
    • M.S. Sansom Alamethicin and related peptaibols - model ion channels Eur. Biophys. J. 22 1993 105 124 (Pubitemid 23275443)
    • (1993) European Biophysics Journal , vol.22 , Issue.2 , pp. 105-124
    • Sansom, M.S.P.1
  • 44
    • 0023887975 scopus 로고
    • Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: Salt and cholesterol effects
    • S. Stankowski, U.D. Schwarz, and G. Schwarz Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: salt and cholesterol effects Biochim. Biophys. Acta 941 1988 11 18
    • (1988) Biochim. Biophys. Acta , vol.941 , pp. 11-18
    • Stankowski, S.1    Schwarz, U.D.2    Schwarz, G.3
  • 45
    • 0037114412 scopus 로고    scopus 로고
    • Characterization of implant materials in fetal bovine serum and sodium sulfate by electrochemical impedance spectroscopy. I. Mechanically polished samples
    • DOI 10.1002/jbm.10329
    • F. Contu, B. Elsener, and H. Bohni Characterization of implant materials in fetal bovine serum and sodium sulfate by electrochemical impedance spectroscopy. I. Mechanically polished samples J. Biomed. Mater. Res. 62 2002 412 421 (Pubitemid 35332205)
    • (2002) Journal of Biomedical Materials Research , vol.62 , Issue.3 , pp. 412-421
    • Contu, F.1    Elsener H Bhni, B.2
  • 47
    • 0021896098 scopus 로고
    • A package for impedance/admittance data analysis
    • B.A. Boukamp A package for impedance/admittance data analysis Solid State Ionics 18 1986 136 140
    • (1986) Solid State Ionics , vol.18 , pp. 136-140
    • Boukamp, B.A.1
  • 48
    • 84867497599 scopus 로고    scopus 로고
    • Electrochemical impedance spectroscopy and atomic force microscopic studies of electrical and mechanical properties of nano-black lipid membranes and size dependence
    • Z.-W. Zhu, Y. Wang, X. Zhang, C.-F. Sun, M.-G. Li, J.-W. Yan, and B.-W. Mao Electrochemical impedance spectroscopy and atomic force microscopic studies of electrical and mechanical properties of nano-black lipid membranes and size dependence Langmuir 28 2012 14739 14746
    • (2012) Langmuir , vol.28 , pp. 14739-14746
    • Zhu, Z.-W.1    Wang, Y.2    Zhang, X.3    Sun, C.-F.4    Li, M.-G.5    Yan, J.-W.6    Mao, B.-W.7
  • 49
    • 0032485744 scopus 로고    scopus 로고
    • Impedance of rough capacitive electrodes: The role of surface disorder
    • PII S0022072898000254
    • Z. Kerner, and T. Pajkossy Impedance of rough capacitive electrodes: the role of surface disorder J. Electroanal. Chem. 448 1998 139 142 (Pubitemid 128411179)
    • (1998) Journal of Electroanalytical Chemistry , vol.448 , Issue.1 , pp. 139-142
    • Kerner, Z.1    Pajkossy, T.2
  • 50
    • 0026031974 scopus 로고
    • Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons
    • S.J. Johnson, T.M. Bayerl, D.C. Mcdermott, G.W. Adam, A.R. Rennie, R.K. Thomas, and E. Sackmann Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons Biophys. J. 59 1991 289 294
    • (1991) Biophys. J. , vol.59 , pp. 289-294
    • Johnson, S.J.1    Bayerl, T.M.2    McDermott, D.C.3    Adam, G.W.4    Rennie, A.R.5    Thomas, R.K.6    Sackmann, E.7
  • 51
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of MSI-78 in lipid bilayers
    • DOI 10.1529/biophysj.105.062596
    • A. Mecke, D.K. Lee, A. Ramamoorthy, B.G. Orr, and M.M.B. Holl Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers Biophys. J. 89 2005 4043 4050 (Pubitemid 41725624)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4043-4050
    • Mecke, A.1    Lee, D.-K.2    Ramamoorthy, A.3    Orr, B.G.4    Banaszak Holl, M.M.5
  • 52
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • DOI 10.1073/pnas.95.16.9541
    • R. Bals, X.R. Wang, M. Zasloff, and J.M. Wilson The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface Proc. Natl. Acad. Sci. U. S. A. 95 1998 9541 9546 (Pubitemid 28506267)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.16 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 53
    • 15044347981 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of antimicrobial peptide-membrane interactions: Affinity & mechanism of action
    • DOI 10.1007/BF02442579
    • K. Hall, H. Mozsolits, and M.I. Aguilar Surface plasmon resonance analysis of antimicrobial peptide-membrane interactions: affinity & mechanism of action Lett. Pept. Sci. 10 2003 475 485 (Pubitemid 40379038)
    • (2003) Letters in Peptide Science , vol.10 , Issue.5-6 , pp. 475-485
    • Hall, K.1    Mozsolits, H.2    Aguilar, M.-I.3
  • 54
    • 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
  • 55
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.02.021, PII S0005273606000733
    • H. Sato, and J.B. Feix Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1245 1256 (Pubitemid 44444829)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 56
    • 0026638245 scopus 로고
    • Impedance spectroscopy
    • J.R. Macdonald Impedance spectroscopy Ann. Biomed. Eng. 20 1992 289 305
    • (1992) Ann. Biomed. Eng. , vol.20 , pp. 289-305
    • Macdonald, J.R.1
  • 57
    • 0022149957 scopus 로고
    • Interfaces as a field for arranging organic-molecules
    • K. Miyano Interfaces as a field for arranging organic-molecules Jpn. J. Appl. Phys. Part 1 24 1985 1379 1388
    • (1985) Jpn. J. Appl. Phys. Part , vol.1 , Issue.24 , pp. 1379-1388
    • Miyano, K.1
  • 58
    • 0024276410 scopus 로고
    • Chemistry of the metal-polymer interfacial region
    • H. Leidheiser, and P.D. Deck Chemistry of the metal-polymer interfacial region Science 241 1988 1176 1181
    • (1988) Science , vol.241 , pp. 1176-1181
    • Leidheiser, H.1    Deck, P.D.2
  • 60
    • 0028149041 scopus 로고
    • Assembly and molecular organization of self-assembled lipid bilayers on solid substrates monitored by surface plasmon resonance spectroscopy
    • DOI 10.1016/0005-2736(94)90266-6
    • Z. Salamon, Y. Wang, G. Tollin, and H.A. Macleod Assembly and molecular-organization of self-assembled lipid bilayers on solid substrates monitored by surface-plasmon resonance spectroscopy Biochim. Biophys. Acta Biomembr. 1195 1994 267 275 (Pubitemid 24331648)
    • (1994) Biochimica et Biophysica Acta - Biomembranes , vol.1195 , Issue.2 , pp. 267-275
    • Salamon, Z.1    Wang, Y.2    Tollin, G.3    Macleod, H.A.4
  • 61
    • 0033633623 scopus 로고    scopus 로고
    • Potential-induced defects in n-alkanethiol self-assembled monolayers monitored by impedance spectroscopy
    • E. Boubour, and R.B. Lennox Potential-induced defects in n-alkanethiol self-assembled monolayers monitored by impedance spectroscopy J. Phys. Chem. B 104 2000 9004 9010
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9004-9010
    • Boubour, E.1    Lennox, R.B.2
  • 62
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • DOI 10.1042/0264-6021:3410501
    • Z. Oren, J.C. Lerman, G.H. Gudmundsson, B. Agerberth, and Y. Shai Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell selective activity Biochem. J. 341 1999 501 513 (Pubitemid 29389178)
    • (1999) Biochemical Journal , vol.341 , Issue.3 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 63
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • DOI 10.1046/j.1365-2796.2003.01228.x
    • H.G. Boman Antibacterial peptides: basic facts and emerging concepts J. Intern. Med. 254 2003 197 215 (Pubitemid 37070221)
    • (2003) Journal of Internal Medicine , vol.254 , Issue.3 , pp. 197-215
    • Boman, H.G.1
  • 65
    • 84868261398 scopus 로고    scopus 로고
    • The use of MALDI-TOF-MS and in silico studies for determination of antimicrobial peptides' affinity to bacterial cells
    • S.M. Mandal, L. Migliolo, and O.L. Franco The use of MALDI-TOF-MS and in silico studies for determination of antimicrobial peptides' affinity to bacterial cells J. Am. Soc. Mass Spectrom. 23 2012 1939 1948
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1939-1948
    • Mandal, S.M.1    Migliolo, L.2    Franco, O.L.3
  • 66
    • 33646870619 scopus 로고    scopus 로고
    • A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin
    • DOI 10.1080/09687860500485303, PII X446000071733
    • A.J. Mason, I.N.H. Chotimah, P. Bertani, and B. Bechinger A spectroscopic study of the membrane interaction of the antimicrobial peptide pleurocidin Mol. Membr. Biol. 23 2006 185 194 (Pubitemid 43786020)
    • (2006) Molecular Membrane Biology , vol.23 , Issue.2 , pp. 185-194
    • Mason, A.J.1    Chotimah, I.N.H.2    Bertani, P.3    Bechinger, B.4
  • 67
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • DOI 10.1021/bi036284s
    • K.A. Henzler-Wildman, G.V. Martinez, M.F. Brown, and A. Ramamoorthy Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37 Biochemistry 43 2004 8459 8469 (Pubitemid 38902524)
    • (2004) Biochemistry , vol.43 , Issue.26 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4


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