메뉴 건너뛰기




Volumn 110, Issue 22, 2013, Pages 8918-8923

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

Author keywords

Antibiotics; De novo protein design; Innate host defense; Nanometrology; Nanoscopy

Indexed keywords

ANTIINFECTIVE AGENT; PHOSPHOLIPID;

EID: 84878432085     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1222824110     Document Type: Article
Times cited : (120)

References (39)
  • 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
  • 3
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki K, Murase O, Fujii N, Miyajima K (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35(35):11361-11368.
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 4
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang L, Harroun TA, Weiss TM, Ding L, Huang HW (2001) Barrel-stave model or toroidal model? A case study on melittin pores. Biophys J 81(3):1475-1485.
    • (2001) Biophys J , vol.81 , Issue.3 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 5
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • Qian S, Wang W, Yang L, Huang HW (2008) Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores. Proc Natl Acad Sci USA 105(45): 17379-17383.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.45 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 6
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki K, Yoneyama S, Miyajima K (1997) Pore formation and translocation of melittin. Biophys J 73(2):831-838.
    • (1997) Biophys J , vol.73 , Issue.2 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 7
    • 34249858459 scopus 로고    scopus 로고
    • AMPer: A database and an automated discovery tool for antimicrobial peptides
    • Fjell CD, Hancock REW, Cherkasov A (2007) AMPer: A database and an automated discovery tool for antimicrobial peptides. Bioinformatics 23(9):1148-1155.
    • (2007) Bioinformatics , vol.23 , Issue.9 , pp. 1148-1155
    • Fjell, C.D.1    Hancock, R.E.W.2    Cherkasov, A.3
  • 8
    • 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.
    • (1996) Biophys J , vol.70 , Issue.6 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 9
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y (1992) Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31(49):12416-12423.
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 10
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang HW (2000) Action of antimicrobial peptides: Two-state model. Biochemistry 39(29):8347-8352.
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 11
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a ß-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • Mani R, et al. (2006) Membrane-dependent oligomeric structure and pore formation of a ß-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proc Natl Acad Sci USA 103(44):16242-16247.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.44 , pp. 16242-16247
    • Mani, R.1
  • 12
    • 33846251959 scopus 로고    scopus 로고
    • Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of a/ß-peptides
    • Schmitt MA, Weisblum B, Gellman SH (2007) Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of a/ß-peptides. J Am Chem Soc 129(2):417-428.
    • (2007) J Am Chem Soc , vol.129 , Issue.2 , pp. 417-428
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 13
    • 84859562228 scopus 로고    scopus 로고
    • Anticancer ß-hairpin peptides: Membrane-induced folding triggers activity
    • Sinthuvanich C, et al. (2012) Anticancer ß-hairpin peptides: Membrane-induced folding triggers activity. J Am Chem Soc 134(14):6210-6217.
    • (2012) J Am Chem Soc , vol.134 , Issue.14 , pp. 6210-6217
    • Sinthuvanich, C.1
  • 14
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • Yang L, Weiss TM, Lehrer RI, Huang HW (2000) Crystallization of antimicrobial pores in membranes: Magainin and protegrin. Biophys J 79(4):2002-2009.
    • (2000) Biophys J , vol.79 , Issue.4 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 15
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock KJ, Lee D-K, Ramamoorthy A (2003) MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys J 84(5):3052-3060.
    • (2003) Biophys J , vol.84 , Issue.5 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 16
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of MSI-78 in lipid bilayers
    • Mecke A, Lee D-K, Ramamoorthy A, Orr BG, Banaszak Holl MM (2005) Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of MSI-78 in lipid bilayers. Biophys J 89(6):4043-4050.
    • (2005) Biophys J , 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
  • 17
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • Lee M-T, Hung W-C, Chen F-Y, Huang HW (2008) Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides. Proc Natl Acad Sci USA 105(13):5087-5092.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.13 , pp. 5087-5092
    • Lee, M.-T.1    Hung, W.-C.2    Chen, F.-Y.3    Huang, H.W.4
  • 18
    • 74849097759 scopus 로고    scopus 로고
    • Vesicle budding induced by a pore-forming peptide
    • Yu Y, Vroman JA, Bae SC, Granick S (2010) Vesicle budding induced by a pore-forming peptide. J Am Chem Soc 132(1):195-201.
    • (2010) J Am Chem Soc , vol.132 , Issue.1 , pp. 195-201
    • Yu, Y.1    Vroman, J.A.2    Bae, S.C.3    Granick, S.4
  • 19
    • 0030741317 scopus 로고    scopus 로고
    • The heptameric prepore of a staphylococcal a-hemolysin mutant in lipid bilayers imaged by atomic force microscopy
    • Fang Y, Cheley S, Bayley H, Yang J (1997) The heptameric prepore of a staphylococcal a-hemolysin mutant in lipid bilayers imaged by atomic force microscopy. Biochemistry 36(31):9518-9522.
    • (1997) Biochemistry , vol.36 , Issue.31 , pp. 9518-9522
    • Fang, Y.1    Cheley, S.2    Bayley, H.3    Yang, J.4
  • 20
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal a-hemolysin, a heptameric transmembrane pore
    • Song L, et al. (1996) Structure of staphylococcal a-hemolysin, a heptameric transmembrane pore. Science 274(5294):1859-1866.
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1
  • 21
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y (2002) Mode of action of membrane active antimicrobial peptides. Biopolymers 66(4):236-248.
    • (2002) Biopolymers , vol.66 , Issue.4 , pp. 236-248
    • Shai, Y.1
  • 22
    • 78549267766 scopus 로고    scopus 로고
    • The structural basis for membrane binding and pore formation by lymphocyte perforin
    • Law RHP, et al. (2010) The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature 468(7322):447-451.
    • (2010) Nature , vol.468 , Issue.7322 , pp. 447-451
    • Law, R.H.P.1
  • 23
    • 78951478570 scopus 로고    scopus 로고
    • Human perforin employs different avenues to damage membranes
    • Praper T, et al. (2011) Human perforin employs different avenues to damage membranes. J Biol Chem 286(4):2946-2955.
    • (2011) J Biol Chem , vol.286 , Issue.4 , pp. 2946-2955
    • Praper, T.1
  • 24
    • 0033607208 scopus 로고    scopus 로고
    • Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of protein A
    • Shea J-E, Onuchic JN, Brooks CL, 3rd (1999) Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of protein A. Proc Natl Acad Sci USA 96(22):12512-12517.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.22 , pp. 12512-12517
    • Shea, J.-E.1    Onuchic, J.N.2    Brooks III, C.L.3
  • 25
    • 77950860384 scopus 로고    scopus 로고
    • Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy
    • Fantner GE, Barbero RJ, Gray DS, Belcher AM (2010) Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy. Nat Nanotechnol 5(4):280-285.
    • (2010) Nat Nanotechnol , vol.5 , Issue.4 , pp. 280-285
    • Fantner, G.E.1    Barbero, R.J.2    Gray, D.S.3    Belcher, A.M.4
  • 27
    • 33646148481 scopus 로고    scopus 로고
    • Lipid asymmetry in DLPC/DSPCsupported lipid bilayers: A combined AFM and fluorescence microscopy study
    • Lin W-C, Blanchette CD, Ratto TV, Longo ML (2006) Lipid asymmetry in DLPC/DSPCsupported lipid bilayers: A combined AFM and fluorescence microscopy study. Biophys J 90(1):228-237.
    • (2006) Biophys J , vol.90 , Issue.1 , pp. 228-237
    • Lin, W.-C.1    Blanchette, C.D.2    Ratto, T.V.3    Longo, M.L.4
  • 28
    • 4444233817 scopus 로고    scopus 로고
    • Using nanotechniques to explore microbial surfaces
    • Dufrêne YF (2004) Using nanotechniques to explore microbial surfaces. Nat Rev Microbiol 2(6):451-460.
    • (2004) Nat Rev Microbiol , vol.2 , Issue.6 , pp. 451-460
    • Dufrêne, Y.F.1
  • 29
    • 33749359415 scopus 로고    scopus 로고
    • Phase separation of lipid membranes analyzed with high-resolution secondary ion mass spectrometry
    • Kraft ML, Weber PK, Longo ML, Hutcheon ID, Boxer SG (2006) Phase separation of lipid membranes analyzed with high-resolution secondary ion mass spectrometry. Science 313(5795):1948-1951.
    • (2006) Science , vol.313 , Issue.5795 , pp. 1948-1951
    • Kraft, M.L.1    Weber, P.K.2    Longo, M.L.3    Hutcheon, I.D.4    Boxer, S.G.5
  • 30
    • 0027394117 scopus 로고
    • Role of calcium in the adhesion and fusion of bilayers
    • Leckband DE, Helm CA, Israelachvili J (1993) Role of calcium in the adhesion and fusion of bilayers. Biochemistry 32(4):1127-1140.
    • (1993) Biochemistry , vol.32 , Issue.4 , pp. 1127-1140
    • Leckband, D.E.1    Helm, C.A.2    Israelachvili, J.3
  • 31
    • 22144486884 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using X-ray scattering from oriented multilamellar arrays and from unilamellar vesicles
    • Ku-cerka N, et al. (2005) Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using X-ray scattering from oriented multilamellar arrays and from unilamellar vesicles. Biophys J 88(4):2626-2637.
    • (2005) Biophys J , vol.88 , Issue.4 , pp. 2626-2637
    • Ku-cerka, N.1
  • 34
    • 28444483198 scopus 로고    scopus 로고
    • Induction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived poreforming peptide
    • Nomura K, et al. (2005) Induction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived poreforming peptide. Biophys J 89(6):4067-4080.
    • (2005) Biophys J , vol.89 , Issue.6 , pp. 4067-4080
    • Nomura, K.1
  • 35
    • 77955777573 scopus 로고    scopus 로고
    • LD spectroscopy of natural and synthetic biomaterials
    • Hicks MR, Kowalski J, Rodger A (2010) LD spectroscopy of natural and synthetic biomaterials. Chem Soc Rev 39(9):3380-3393.
    • (2010) Chem Soc Rev , vol.39 , Issue.9 , pp. 3380-3393
    • Hicks, M.R.1    Kowalski, J.2    Rodger, A.3
  • 37
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda JB, et al. (2010) Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types. J Phys Chem B 114(23):7830-7843.
    • (2010) J Phys Chem B , vol.114 , Issue.23 , pp. 7830-7843
    • Klauda, J.B.1
  • 38
    • 84878461691 scopus 로고    scopus 로고
    • Imaging secondary ion mass spectroscopy
    • Wiley-VCH, Weinheim, Germany
    • Moore KL, Schröder M, Grovenor CRM (2012) Imaging secondary ion mass spectroscopy. Handbook of Nanoscopy (Wiley-VCH, Weinheim, Germany), pp 709-744.
    • (2012) Handbook of Nanoscopy , pp. 709-744
    • Moore, K.L.1    Schröder, M.2    Grovenor, C.R.M.3
  • 39
    • 0032844969 scopus 로고    scopus 로고
    • Dynamics of transient pores in stretched vesicles
    • Sandre O, Moreaux L, Brochard-Wyart F (1999) Dynamics of transient pores in stretched vesicles. Proc Natl Acad Sci USA 96(19):10591-10596.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.19 , pp. 10591-10596
    • Sandre, O.1    Moreaux, L.2    Brochard-Wyart, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.