메뉴 건너뛰기




Volumn 109, Issue 52, 2012, Pages 21223-21227

Direct visualization of the alamethicin pore formed in a planar phospholipid matrix

Author keywords

Antimicrobial; Interface; Langmuir Blodgett

Indexed keywords

ALAMETHICIN; NANOCRYSTAL; PEPTIDE; PHOSPHOLIPID; WATER;

EID: 84871832622     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201559110     Document Type: Article
Times cited : (89)

References (38)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415(6870):389-395.
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock REW (2001) Cationic peptides: Effectors in innate immunity and novel antimicrobials. Lancet Infect Dis 1(3):156-164.
    • (2001) Lancet Infect Dis , vol.1 , Issue.3 , pp. 156-164
    • Hancock, R.E.W.1
  • 4
    • 0014203489 scopus 로고
    • A polypeptide antibacterial agent isolated from Trichoderma viride
    • Meyer CE, Reusser F (1967) A polypeptide antibacterial agent isolated from Trichoderma viride. Experientia 23(2):85-86.
    • (1967) Experientia , vol.23 , Issue.2 , pp. 85-86
    • Meyer, C.E.1    Reusser, F.2
  • 5
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • Marsh D (1996) Peptide models for membrane channels. Biochem J 315(Pt 2):345-361.
    • (1996) Biochem J , vol.315 , Issue.PART 2 , pp. 345-361
    • Marsh, D.1
  • 6
    • 34447322795 scopus 로고    scopus 로고
    • The history of Alamethicin: A review of the most extensively studied peptaibol
    • DOI 10.1002/cbdv.200790095
    • Leitgeb B, Szekeres A, Manczinger L, Vágvölgyi C, Kredics L (2007) The history of alamethicin: A review of the most extensively studied peptaibol. Chem Biodivers 4(6):1027-1051. (Pubitemid 47072862)
    • (2007) Chemistry and Biodiversity , vol.4 , Issue.6 , pp. 1027-1051
    • Leitgeb, B.1    Szekeres, A.2    Manczinger, L.3    Vagvolgyi, C.4    Kredics, L.5
  • 7
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution
    • Fox RO, Jr., Richards FM (1982) A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution. Nature 300(5890):325-330.
    • (1982) Nature , vol.300 , Issue.5890 , pp. 325-330
    • Fox Jr., R.O.1    Richards, F.M.2
  • 9
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
    • Vogel H (1987) Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes. Biochemistry 26(14):4562-4572.
    • (1987) Biochemistry , vol.26 , Issue.14 , pp. 4562-4572
    • Vogel, H.1
  • 10
    • 0024291269 scopus 로고
    • Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin
    • Haris PI, Chapman D (1988) Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin. Biochim Biophys Acta 943(2):375-380.
    • (1988) Biochim Biophys Acta , vol.943 , Issue.2 , pp. 375-380
    • Haris, P.I.1    Chapman, D.2
  • 11
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols - Model ion channels
    • Sansom MSP (1993) Alamethicin and related peptaibols - model ion channels. Eur Biophys J 22(2):105-124.
    • (1993) Eur Biophys J , vol.22 , Issue.2 , pp. 105-124
    • Sansom, M.S.P.1
  • 12
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He K, Ludtke SJ, Worcester DL, Huang HW (1996) Neutron scattering in the plane of membranes: Structure of alamethicin pores. Biophys J 70(6):2659-2666. (Pubitemid 26000964)
    • (1996) Biophysical Journal , vol.70 , Issue.6 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 13
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang HW (2006) Molecular mechanism of antimicrobial peptides: The origin of cooperativity. Biochim Biophys Acta 1758(9):1292-1302.
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.9 , pp. 1292-1302
    • Huang, H.W.1
  • 14
    • 0025889072 scopus 로고
    • Lipid-alamethicin interactions influence alamethicin orientation
    • Huang HW, Wu Y (1991) Lipid-alamethicin interactions influence alamethicin orientation. Biophys J 60(5):1079-1087.
    • (1991) Biophys J , vol.60 , Issue.5 , pp. 1079-1087
    • Huang, H.W.1    Wu, Y.2
  • 15
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger B (1997) Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin. J Membr Biol 156(3):197-211.
    • (1997) J Membr Biol , vol.156 , Issue.3 , pp. 197-211
    • Bechinger, B.1
  • 16
    • 0029072985 scopus 로고
    • Packing interactions of Aib-containing helices: Molecular modeling of parallel dimers of simple hydrophobic helices and of alamethicin
    • Breed J, Kerr ID, Sankararamakrishnan R, Sansom MSP (1995) Packing interactions of Aib-containing helices: Molecular modeling of parallel dimers of simple hydrophobic helices and of alamethicin. Biopolymers 35(6):639-655.
    • (1995) Biopolymers , vol.35 , Issue.6 , pp. 639-655
    • Breed, J.1    Kerr, I.D.2    Sankararamakrishnan, R.3    Sansom, M.S.P.4
  • 17
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley GA, Wallace BA (1992) Model ion channels: Gramicidin and alamethicin. J Membr Biol 129(2):109-136.
    • (1992) J Membr Biol , vol.129 , Issue.2 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 18
    • 0020584793 scopus 로고
    • A helix dipole model for alamethicin and related transmembrane channels
    • DOI 10.1016/0014-5793(83)81105-3
    • Mathew MK, Balaram P (1983) A helix dipole model for alamethicin and related transmembrane channels. FEBS Lett 157(1):1-5. (Pubitemid 13072144)
    • (1983) FEBS Letters , vol.157 , Issue.1 , pp. 1-5
    • Mathew, M.K.1    Balaram, P.2
  • 19
    • 0023754246 scopus 로고
    • Conformation of alamethicin in phospholipid vesicles: Implications for insertion models
    • Cascio M, Wallace BA (1988) Conformation of alamethicin in phospholipid vesicles: Implications for insertion models. Proteins 4(2):89-98.
    • (1988) Proteins , vol.4 , Issue.2 , pp. 89-98
    • Cascio, M.1    Wallace, B.A.2
  • 20
    • 70350031590 scopus 로고    scopus 로고
    • Alamethicin aggregation in lipid membranes
    • Pan J, Tristram-Nagle S, Nagle JF (2009) Alamethicin aggregation in lipid membranes. J Membr Biol 231(1):11-27.
    • (2009) J Membr Biol , vol.231 , Issue.1 , pp. 11-27
    • Pan, J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 21
    • 33748940257 scopus 로고    scopus 로고
    • Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering
    • DOI 10.1016/j.bbamem.2006.08.002, PII S0005273606002951
    • Salditt T, Li C, Spaar A (2006) Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering. Biochim Biophys Acta 1758(9):1483-1498. (Pubitemid 44436089)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1483-1498
    • Salditt, T.1    Li, C.2    Spaar, A.3
  • 22
    • 34250373778 scopus 로고    scopus 로고
    • Interaction of alamethicin pores in DMPC bilayers
    • DOI 10.1529/biophysj.106.101204
    • Constantin D, Brotons G, Jarre A, Li C, Salditt T (2007) Interaction of alamethicin pores in DMPC bilayers. Biophys J 92(11):3978-3987. (Pubitemid 46910584)
    • (2007) Biophysical Journal , vol.92 , Issue.11 , pp. 3978-3987
    • Constantin, D.1    Brotons, G.2    Jarre, A.3    Li, C.4    Salditt, T.5
  • 23
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He K, Ludtke SJ, Heller WT, Huang HW (1996) Mechanism of alamethicin insertion into lipid bilayers. Biophys J 71(5):2669-2679. (Pubitemid 26367729)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 24
    • 0025989688 scopus 로고
    • Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase?
    • Wang J, Pullman A (1991) Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase? Biochim Biophys Acta 1070(2):493-496.
    • (1991) Biochim Biophys Acta , vol.1070 , Issue.2 , pp. 493-496
    • Wang, J.1    Pullman, A.2
  • 25
    • 58949093974 scopus 로고    scopus 로고
    • Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs
    • Cheng JTJ, Hale JD, Elliot M, Hancock REW, Straus SK (2009) Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys J 96(2):552-565.
    • (2009) Biophys J , vol.96 , Issue.2 , pp. 552-565
    • Cheng, J.T.J.1    Hale, J.D.2    Elliot, M.3    Hancock, R.E.W.4    Straus, S.K.5
  • 26
    • 0022498409 scopus 로고
    • Membrane lipid composition of obligately and facultatively alkalophilic strains of Bacillus spp.
    • Clejan S, Krulwich TA, Mondrus KR, Seto-Young D (1986) Membrane lipid composition of obligately and facultatively alkalophilic strains of Bacillus spp. J Bacteriol 168(1):334-340. (Pubitemid 16001620)
    • (1986) Journal of Bacteriology , vol.168 , Issue.1 , pp. 334-340
    • Clejan, S.1    Krulwich, T.A.2    Mondrus, K.R.3    Seto-Young, D.4
  • 27
    • 70149109995 scopus 로고    scopus 로고
    • Molecular resolution imaging of an antibiotic peptide in a lipid matrix
    • Sek S, Laredo T, Dutcher JR, Lipkowski J (2009) Molecular resolution imaging of an antibiotic peptide in a lipid matrix. J Am Chem Soc 131(18):6439-6444.
    • (2009) J Am Chem Soc , vol.131 , Issue.18 , pp. 6439-6444
    • Sek, S.1    Laredo, T.2    Dutcher, J.R.3    Lipkowski, J.4
  • 30
    • 1042286134 scopus 로고
    • Structural characterization and nanometer-scale domain formation in a model phospholipid bilayer as determined by infrared spectroscopy and scanning tunneling microscopy
    • Gregory BW, Dluhy RA, Bottomley LA (1994) Structural characterization and nanometer-scale domain formation in a model phospholipid bilayer as determined by infrared spectroscopy and scanning tunneling microscopy. J Phys Chem 98(3):1010-1021.
    • (1994) J Phys Chem , vol.98 , Issue.3 , pp. 1010-1021
    • Gregory, B.W.1    Dluhy, R.A.2    Bottomley, L.A.3
  • 31
    • 0034043224 scopus 로고    scopus 로고
    • Asymmetrical ion-channel model inferred from two-dimensional crystallization of a peptide antibiotic
    • Ionov R, El-Abed A, Angelova A, Goldmann M, Peretti P (2000) Asymmetrical ionchannel model inferred from two-dimensional crystallization of a peptide antibiotic. Biophys J 78(6):3026-3035. (Pubitemid 30396933)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 3026-3035
    • Ionov, R.1    El-Abed, A.2    Angelova, A.3    Goldmann, M.4    Peretti, P.5
  • 32
    • 33244492681 scopus 로고    scopus 로고
    • Phase behavior of mixed langmuir monolayers from amphiphilic block copolymers and an antimicrobial peptide
    • DOI 10.1021/la0524216
    • Haefele T, Kita-Tokarczyk K, Meier W (2006) Phase behavior of mixed Langmuir monolayers from amphiphilic block copolymers and an antimicrobial peptide. Langmuir 22(3):1164-1172. (Pubitemid 43282175)
    • (2006) Langmuir , vol.22 , Issue.3 , pp. 1164-1172
    • Haefele, T.1    Kita-Tokarczyk, K.2    Meier, W.3
  • 33
    • 0000829678 scopus 로고    scopus 로고
    • Scanning Tunneling and Atomic Force Microscopy Probes of Self-Assembled, Physisorbed Monolayers: Peeking at the Peaks
    • Giancarlo LC, Flynn GW (1998) Scanning tunneling and atomic force microscopy probes of self-assembled, physisorbed monolayers: Peeking at the peaks. Annu Rev Phys Chem 49:297-336. (Pubitemid 128436893)
    • (1998) Annual Review of Physical Chemistry , vol.49 , Issue.1 , pp. 297-336
    • Giancarlo, L.C.1    Flynn, G.W.2
  • 34
    • 0037206704 scopus 로고    scopus 로고
    • The role of hydrophobic chains in self-assembly at electrified interfaces: Observation of potential-induced transformations of two-dimensional crystals of hexadecane by in-situ scanning tunneling microscopy
    • DOI 10.1021/jp021106e
    • He YF, Ye T, Borguet E (2002) The role of hydrophobic chains in self-assembly at electrified interfaces: Observation of potential-induced transformations of two-dimensional crystals of hexadecane by in-situ scanning tunneling microscopy. J Phys Chem B 106(43):11264-11271. (Pubitemid 35313766)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.43 , pp. 11264-11271
    • He, Y.1    Ye, T.2    Borguet, E.3
  • 35
    • 14544306931 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the phase behavior and organization of lipid bilayer model membranes composed of binary mixtures of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol
    • DOI 10.1016/j.bbamem.2004.12.007
    • Lewis RNAH, Zhang Y-P, McElhaney RN (2005) Calorimetric and spectroscopic studies of the phase behavior and organization of lipid bilayer model membranes composed of binary mixtures of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol. Biochim Biophys Acta 1668(2):203-214. (Pubitemid 40298924)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1668 , Issue.2 , pp. 203-214
    • Lewis, R.N.A.H.1    Zhang, Y.-P.2    McElhaney, R.N.3
  • 36
    • 0021388240 scopus 로고
    • ELECTRON MICROSCOPY AND DIFFRACTION STUDY OF PHOSPHOLIPID MONOLAYERS TRANSFERRED FROM WATER TO SOLID SUBSTRATES.
    • Fischer A, Sackmann E (1984) Electron-microscopy and diffraction study of phospholipid monolayers transferred from water to solid substrates. J Phys (Paris) 45(3):517-527. (Pubitemid 14544527)
    • (1984) Journal de physique Paris , vol.45 , Issue.3 , pp. 517-527
    • Fischer, A.1    Sackmann, E.2
  • 37
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • Tieleman DP, Berendsen HJC, Sansom MSP (1999) An alamethicin channel in a lipid bilayer: Molecular dynamics simulations. Biophys J 76(4):1757-1769. (Pubitemid 29266335)
    • (1999) Biophysical Journal , vol.76 , Issue.4 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 38
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman DP, Hess B, Sansom MSP (2002) Analysis and evaluation of channel models: Simulations of alamethicin. Biophys J 83(5):2393-2407. (Pubitemid 35265736)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2393-2407
    • Peter, T.D.1    Hess, B.2    Sansom, M.S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.