메뉴 건너뛰기




Volumn 36, Issue 4-5, 2007, Pages 305-314

Leakage and lysis of lipid membranes induced by the lipopeptide surfactin

Author keywords

Antibiotic peptide; Asymmetric partitioning; Calcein leakage; Membrane lysis; Membrane permeabilization

Indexed keywords

ANTIBIOTIC AGENT; CALCEIN; DETERGENT; LIPID; LIPOPEPTIDE; SURFACTIN; WATER;

EID: 34247192572     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-006-0091-5     Document Type: Article
Times cited : (175)

References (44)
  • 1
    • 0018899158 scopus 로고
    • Serum-induced leakage of liposome contents
    • Allen TM, Cleland LG (1980) Serum-induced leakage of liposome contents. Biochim Biophys Acta 597:418-426
    • (1980) Biochim Biophys Acta , vol.597 , pp. 418-426
    • Allen, T.M.1    Cleland, L.G.2
  • 2
    • 0031060732 scopus 로고    scopus 로고
    • Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes
    • Beven L, Wroblewski H (1997) Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes. Res Microbiol 148:163-175
    • (1997) Res Microbiol , vol.148 , pp. 163-175
    • Beven, L.1    Wroblewski, H.2
  • 3
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes
    • Binder H, Lindblom G (2003) Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys J 85:982-995
    • (2003) Biophys J , vol.85 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 4
    • 2942560687 scopus 로고    scopus 로고
    • Recent applications of biosurfactants as biological and immunological molecules
    • Cameotra SS, Makkar RS (2004) Recent applications of biosurfactants as biological and immunological molecules. Curr Opin Microbiol 7:262-266
    • (2004) Curr Opin Microbiol , vol.7 , pp. 262-266
    • Cameotra, S.S.1    Makkar, R.S.2
  • 5
    • 0037376739 scopus 로고    scopus 로고
    • Molecular mechanism of membrane permeabilization by the peptide antibiotic surfactin
    • Carrillo C, Teruel JA, Aranda FJ, Ortiz A (2003) Molecular mechanism of membrane permeabilization by the peptide antibiotic surfactin. Biochim Biophys Acta Biomembr 1611:91-97
    • (2003) Biochim Biophys Acta Biomembr , vol.1611 , pp. 91-97
    • Carrillo, C.1    Teruel, J.A.2    Aranda, F.J.3    Ortiz, A.4
  • 6
    • 0033277339 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: Biological applications
    • Chellani M (1999) Isothermal titration calorimetry: biological applications. Am Biotechnol Lab 17:14-18
    • (1999) Am Biotechnol Lab , vol.17 , pp. 14-18
    • Chellani, M.1
  • 7
    • 0028172066 scopus 로고
    • Vesicle-micelle structural transition of phosphatidylcholine bilayers and Triton X-100
    • De la Maza A, Parra JL (1994) Vesicle-micelle structural transition of phosphatidylcholine bilayers and Triton X-100. Biochem J 303:907-914
    • (1994) Biochem J , vol.303 , pp. 907-914
    • De la Maza, A.1    Parra, J.L.2
  • 8
  • 9
    • 0026253649 scopus 로고
    • Solubilization of lecithin vesicles by C12E8 - structural transitions and temperature effects
    • Edwards K, Almgren M (1991) Solubilization of lecithin vesicles by C12E8 - structural transitions and temperature effects. J Colloid Interface Sci 147:1-21
    • (1991) J Colloid Interface Sci , vol.147 , pp. 1-21
    • Edwards, K.1    Almgren, M.2
  • 10
    • 49049139427 scopus 로고
    • Evaluation of partition constants in compartmentalized systems from fluorescence quenching data
    • Encinas M, Lissi E (1982) Evaluation of partition constants in compartmentalized systems from fluorescence quenching data. Chem Phys Lett 91:55-57
    • (1982) Chem Phys Lett , vol.91 , pp. 55-57
    • Encinas, M.1    Lissi, E.2
  • 11
    • 0034955598 scopus 로고    scopus 로고
    • Membrane stress and permeabilization induced by asymmetric incorporation of compounds
    • Heerklotz H (2001) Membrane stress and permeabilization induced by asymmetric incorporation of compounds. Biophys J 81:184-195
    • (2001) Biophys J , vol.81 , pp. 184-195
    • Heerklotz, H.1
  • 12
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H (2002) Triton promotes domain formation in lipid raft mixtures. Biophys J 83:2693-2701
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 13
    • 0034068626 scopus 로고    scopus 로고
    • Correlation of membrane/water partition coefficients of detergents with the critical micelle concentration
    • Heerklotz H, Seelig J (2000a) Correlation of membrane/water partition coefficients of detergents with the critical micelle concentration. Biophys J 78:2435-2440
    • (2000) Biophys J , vol.78 , pp. 2435-2440
    • Heerklotz, H.1    Seelig, J.2
  • 14
    • 0034707081 scopus 로고    scopus 로고
    • Titration calorimetry of surfactant-membrane partitioning and membrane solubilization
    • Heerklotz H, Seelig J (2000b) Titration calorimetry of surfactant-membrane partitioning and membrane solubilization. Biochim Biophys Acta 1508:69-85
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 69-85
    • Heerklotz, H.1    Seelig, J.2
  • 15
    • 0034859349 scopus 로고    scopus 로고
    • Detergent-like action of the antibiotic peptide surfactin on lipid membranes
    • Heerklotz H, Seelig J (2001) Detergent-like action of the antibiotic peptide surfactin on lipid membranes. Biophys J 81:1547-1554
    • (2001) Biophys J , vol.81 , pp. 1547-1554
    • Heerklotz, H.1    Seelig, J.2
  • 16
    • 0028598233 scopus 로고
    • Membrane/water partition of oligo (ethylene oxide) dodecyl ethers and its relevance for solubilization
    • Heerklotz H, Binder H, Lantzsch G, Klose G (1994) Membrane/water partition of oligo (ethylene oxide) dodecyl ethers and its relevance for solubilization. Biochim Biophys Acta 1196:114-122
    • (1994) Biochim Biophys Acta , vol.1196 , pp. 114-122
    • Heerklotz, H.1    Binder, H.2    Lantzsch, G.3    Klose, G.4
  • 17
    • 0001292725 scopus 로고
    • Application of isothermal titration calorimetry for detecting lipid membrane solubilization
    • Heerklotz H, Lantzsch G, Binder H, Klose G, Blume A (1995) Application of isothermal titration calorimetry for detecting lipid membrane solubilization. Chem Phys Lett 235:517-520
    • (1995) Chem Phys Lett , vol.235 , pp. 517-520
    • Heerklotz, H.1    Lantzsch, G.2    Binder, H.3    Klose, G.4    Blume, A.5
  • 18
    • 33748588716 scopus 로고    scopus 로고
    • Thermodynamic characterization of dilute aqueous lipid/detergent mixtures of POPC and C12EO8 by means of isothermal titration calorimetry
    • Heerklotz H, Lantzsch G, Binder H, Klose G, Blume A (1996) Thermodynamic characterization of dilute aqueous lipid/detergent mixtures of POPC and C12EO8 by means of isothermal titration calorimetry. J Phys Chem 100:6764-6774
    • (1996) J Phys Chem , vol.100 , pp. 6764-6774
    • Heerklotz, H.1    Lantzsch, G.2    Binder, H.3    Klose, G.4    Blume, A.5
  • 19
    • 0030825023 scopus 로고    scopus 로고
    • Lipid/detergent interaction thermodynamics as a function of molecular shape
    • Heerklotz H, Binder H, Lantzsch G, Klose G, Blume A (1997) Lipid/detergent interaction thermodynamics as a function of molecular shape. J Phys Chem B 101:639-645
    • (1997) J Phys Chem B , vol.101 , pp. 639-645
    • Heerklotz, H.1    Binder, H.2    Lantzsch, G.3    Klose, G.4    Blume, A.5
  • 20
    • 2342582833 scopus 로고    scopus 로고
    • Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR
    • Heerklotz H, Wieprecht T, Seelig J (2004) Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. J Phys Chem B 108:4909-4915
    • (2004) J Phys Chem B , vol.108 , pp. 4909-4915
    • Heerklotz, H.1    Wieprecht, T.2    Seelig, J.3
  • 21
    • 0037007359 scopus 로고    scopus 로고
    • Bile salt-induced solubilization of synthetic phosphatidylcholine vesicles studied by isothermal titration calorimetry
    • Hildebrand A, Neubert R, Garidel P, Blume A (2002) Bile salt-induced solubilization of synthetic phosphatidylcholine vesicles studied by isothermal titration calorimetry. Langmuir 18:2836-2847
    • (2002) Langmuir , vol.18 , pp. 2836-2847
    • Hildebrand, A.1    Neubert, R.2    Garidel, P.3    Blume, A.4
  • 22
    • 0016159471 scopus 로고
    • Antitumor activity of Bacillus natto. V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311
    • Kameda Y, Oira S, Matsui K, Kanatomo S, Hase T (1974) Antitumor activity of Bacillus natto. V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311. Chem Pharm Bull (Tokyo) 22:938-944
    • (1974) Chem Pharm Bull (Tokyo) , vol.22 , pp. 938-944
    • Kameda, Y.1    Oira, S.2    Matsui, K.3    Kanatomo, S.4    Hase, T.5
  • 23
    • 0030961843 scopus 로고    scopus 로고
    • Thermodynamics of interaction of octyl glucoside with phosphatidylcholine vesicles: Partitioning and solubilization as studied by high sensitivity titration calorimetry
    • Keller M, Kerth A, Blume A (1997) Thermodynamics of interaction of octyl glucoside with phosphatidylcholine vesicles: partitioning and solubilization as studied by high sensitivity titration calorimetry. Biochim Biophys Acta 1326:178-192
    • (1997) Biochim Biophys Acta , vol.1326 , pp. 178-192
    • Keller, M.1    Kerth, A.2    Blume, A.3
  • 24
    • 0042838043 scopus 로고    scopus 로고
    • Rapid surface motility in Bacillus subtilis is dependent on extracellular surfactin and potassium ion
    • Kinsinger RF, Shirk MC, Fall R (2003) Rapid surface motility in Bacillus subtilis is dependent on extracellular surfactin and potassium ion. J Bacteriol 185:5627-5631
    • (2003) J Bacteriol , vol.185 , pp. 5627-5631
    • Kinsinger, R.F.1    Shirk, M.C.2    Fall, R.3
  • 25
    • 0032767622 scopus 로고    scopus 로고
    • Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives
    • Kracht M, Rokos H, Ozel M, Kowall M, Pauli G, Vater J (1999) Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives. J Antibiot (Tokyo) 52:613-619
    • (1999) J Antibiot (Tokyo) , vol.52 , pp. 613-619
    • Kracht, M.1    Rokos, H.2    Ozel, M.3    Kowall, M.4    Pauli, G.5    Vater, J.6
  • 26
    • 0035479424 scopus 로고    scopus 로고
    • Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin AS, White SH (2001) 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim Biophys Acta 1514:253-260
    • (2001) Biochim Biophys Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 27
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • Ladokhin AS, Wimley WC, White SH (1995) Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching. Biophys J 69:1964-1971
    • (1995) Biophys J , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 28
    • 0019797752 scopus 로고
    • The rate of transmembrane movement of cholesterol in the human erythrocyte
    • Lange Y, Dolde J, Steck TL (1981) The rate of transmembrane movement of cholesterol in the human erythrocyte. J Biol Chem 256:5321-5323
    • (1981) J Biol Chem , vol.256 , pp. 5321-5323
    • Lange, Y.1    Dolde, J.2    Steck, T.L.3
  • 29
    • 0021111031 scopus 로고
    • Solubilization of phospholipids by detergents. Structural and kinetic aspects
    • Lichtenberg D, Robson RJ, Dennis EA (1983) Solubilization of phospholipids by detergents. Structural and kinetic aspects. Biochim Biophys Acta 737:285-304
    • (1983) Biochim Biophys Acta , vol.737 , pp. 285-304
    • Lichtenberg, D.1    Robson, R.J.2    Dennis, E.A.3
  • 30
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D, Goni FM, Heerklotz H (2005) Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem Sci 30:430-436
    • (2005) Trends Biochem Sci , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 31
    • 0001770049 scopus 로고    scopus 로고
    • Membrane interactions of hemolytic and antibacterial peptides
    • Lohner K, Epand R (1997) Membrane interactions of hemolytic and antibacterial peptides. Adv Biophys Chem 6:53-66
    • (1997) Adv Biophys Chem , vol.6 , pp. 53-66
    • Lohner, K.1    Epand, R.2
  • 33
    • 0034695109 scopus 로고    scopus 로고
    • Acceleration of phospholipid flip-flop in the erythrocyte membrane by detergents differing in polar head group and alkyl chain length
    • Pantaler E, Kamp D, Haest CW (2000) Acceleration of phospholipid flip-flop in the erythrocyte membrane by detergents differing in polar head group and alkyl chain length. Biochim Biophys Acta 1509:397-408
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 397-408
    • Pantaler, E.1    Kamp, D.2    Haest, C.W.3
  • 34
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100, octyl glucoside, and sodium cholate
    • Paternostre MT, Roux M, Rigaud JL (1988) Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100, octyl glucoside, and sodium cholate. Biochemistry 27:2668-2677
    • (1988) Biochemistry , vol.27 , pp. 2668-2677
    • Paternostre, M.T.1    Roux, M.2    Rigaud, J.L.3
  • 35
    • 0035830591 scopus 로고    scopus 로고
    • Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes
    • Prenner EJ, Lewis RN, Jelokhani-Niaraki M, Hodges RS, McElhaney RN (2001) Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes. Biochim Biophys Acta 1510:83-92
    • (2001) Biochim Biophys Acta , vol.1510 , pp. 83-92
    • Prenner, E.J.1    Lewis, R.N.2    Jelokhani-Niaraki, M.3    Hodges, R.S.4    McElhaney, R.N.5
  • 36
    • 0034044039 scopus 로고    scopus 로고
    • Endocytosis switch controlled by transmembrane osmotic pressure and phospholipid number asymmetry
    • Rauch C, Farge E (2000) Endocytosis switch controlled by transmembrane osmotic pressure and phospholipid number asymmetry. Biophys J 78:3036-3047
    • (2000) Biophys J , vol.78 , pp. 3036-3047
    • Rauch, C.1    Farge, E.2
  • 37
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz MP, Singer SJ (1974) Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc Natl Acad Sci USA 71:4457-4461
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 38
    • 0024745128 scopus 로고
    • Vesicle-micelle transition of phosphatidylcholine and octyl glucoside elucidated by cryo-transmission electron-microscopy
    • Vinson PK, Talmon Y, Walter A (1989) Vesicle-micelle transition of phosphatidylcholine and octyl glucoside elucidated by cryo-transmission electron-microscopy. Biophys J 56:669-681
    • (1989) Biophys J , vol.56 , pp. 669-681
    • Vinson, P.K.1    Talmon, Y.2    Walter, A.3
  • 39
    • 0031234420 scopus 로고    scopus 로고
    • Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis
    • Vollenbroich D, Ozel M, Vater J, Kamp RM, Pauli G (1997a) Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis. Biologicals 25:289-297
    • (1997) Biologicals , vol.25 , pp. 289-297
    • Vollenbroich, D.1    Ozel, M.2    Vater, J.3    Kamp, R.M.4    Pauli, G.5
  • 40
    • 0031015251 scopus 로고    scopus 로고
    • Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilis
    • Vollenbroich D, Pauli G, Ozel M, Vater J (1997b) Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilis. Appl Environ Microbiol 63:44-49
    • (1997) Appl Environ Microbiol , vol.63 , pp. 44-49
    • Vollenbroich, D.1    Pauli, G.2    Ozel, M.3    Vater, J.4
  • 41
    • 0031163529 scopus 로고    scopus 로고
    • Vesicle-micelle transformation of phosphatidylcholine/octyl-beta-D-glucopyranoside mixtures as detected with titration calorimetry
    • Wenk MR, Seelig J (1997) Vesicle-micelle transformation of phosphatidylcholine/octyl-beta-D-glucopyranoside mixtures as detected with titration calorimetry. J Phys Chem B 101:5224-5231
    • (1997) J Phys Chem B , vol.101 , pp. 5224-5231
    • Wenk, M.R.1    Seelig, J.2
  • 42
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T, Dathe M, Epand RM, Beyermann M, Krause E, Maloy WL, MacDonald DL, Bienert M (1997) Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 36:12869-12880
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 43
    • 0033543167 scopus 로고    scopus 로고
    • Binding of antibacterial magainin peptides to electrically neutral membranes: Thermodynamics and structure
    • Wieprecht T, Beyermann M, Seelig J (1999) Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure. Biochemistry 38:10377-10387
    • (1999) Biochemistry , vol.38 , pp. 10377-10387
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 44
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects
    • Wieprecht T, Apostolov O, Beyermann M, Seelig J (2000) Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects. Biochemistry 39:442-452
    • (2000) Biochemistry , vol.39 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.