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Volumn 120, Issue 6, 1996, Pages 1130-1140

Selective interaction of synthetic antimicrobial peptides derived from sapecin B with lipid bilayers

Author keywords

Amphiphilicity; Antimicrobial peptide; Liposome; Planar bilayer; Selective toxicity

Indexed keywords

AMPHOPHILE; ANTIINFECTIVE AGENT; CARBOXYFLUORESCEIN; CATION; CHLORIDE ION; ION CHANNEL; LIPID; LIPOSOME; PEPTIDE; PHOSPHATE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID; SAPECIN B; UNCLASSIFIED DRUG;

EID: 0030463135     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021532     Document Type: Article
Times cited : (9)

References (54)
  • 1
    • 0023692422 scopus 로고
    • Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina
    • Matsuyama, K. and Natori, S. (1988) Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina. J. Biol. Chem. 263, 17112-17116
    • (1988) J. Biol. Chem. , vol.263 , pp. 17112-17116
    • Matsuyama, K.1    Natori, S.2
  • 2
    • 0027409883 scopus 로고
    • Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: Similarity of sapecin B to charybdotoxin
    • Yamada, K. and Natori, S. (1993) Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin. Biochem. J. 291, 275-279
    • (1993) Biochem. J. , vol.291 , pp. 275-279
    • Yamada, K.1    Natori, S.2
  • 3
    • 0028299333 scopus 로고
    • Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly)
    • Yamada, K. and Natori, S. (1994) Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly). Biochem. J. 298, 623-628
    • (1994) Biochem. J. , vol.298 , pp. 623-628
    • Yamada, K.1    Natori, S.2
  • 4
    • 0028088351 scopus 로고
    • Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus
    • Alvarez-Bravo, J., Kurata, S., and Natori, S. (1994) Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. Biochem. J. 302, 535-538
    • (1994) Biochem. J. , vol.302 , pp. 535-538
    • Alvarez-Bravo, J.1    Kurata, S.2    Natori, S.3
  • 5
    • 0025756511 scopus 로고
    • Formation of ion channels in planar lipid bilayer membranes by synthetic basic peptides
    • Anzai, K., Hamasuna, M., Kadono, H., Lee, S., Aoyagi, H., and Kirino, Y. (1991) Formation of ion channels in planar lipid bilayer membranes by synthetic basic peptides. Biochim. Biophys. Acta 1064, 256-266
    • (1991) Biochim. Biophys. Acta , vol.1064 , pp. 256-266
    • Anzai, K.1    Hamasuna, M.2    Kadono, H.3    Lee, S.4    Aoyagi, H.5    Kirino, Y.6
  • 6
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic α-helical model peptides of various chain lengths
    • Agawa, Y., Lee, S., Ono, S., Aoyagi, H., Ohno, M., Taniguchi, T., Anzai, K., and Kirino, Y. (1991) Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic α-helical model peptides of various chain lengths. J. Biol. Chem. 266, 20218-20222
    • (1991) J. Biol. Chem. , vol.266 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Ohno, M.5    Taniguchi, T.6    Anzai, K.7    Kirino, Y.8
  • 7
    • 0027327036 scopus 로고
    • Effects of salts on conformational change of basic amphipathic peptides from β-structure to α-helix in the presence of phospholipid liposomes and their channel-forming ability
    • Lee, S., Iwata, T., Oyagi, H., Aoyagi, H., Ohno, M., Anzai, K., Kirino, Y., and Sugihara, G. (1993) Effects of salts on conformational change of basic amphipathic peptides from β-structure to α-helix in the presence of phospholipid liposomes and their channel-forming ability. Biochim. Biophys. Acta 1151, 76-82
    • (1993) Biochim. Biophys. Acta , vol.1151 , pp. 76-82
    • Lee, S.1    Iwata, T.2    Oyagi, H.3    Aoyagi, H.4    Ohno, M.5    Anzai, K.6    Kirino, Y.7    Sugihara, G.8
  • 9
    • 0028296746 scopus 로고
    • Two mode ion channels induced by interaction of acidic amphipathic α-helical peptides with lipid bilayers
    • Lee, S., Tanaka, T., Anzai, K., Kirino, Y., Aoyagi, H., and Sugihara, G. (1994) Two mode ion channels induced by interaction of acidic amphipathic α-helical peptides with lipid bilayers. Biochim. Biophys. Acta 1191, 181-189
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 181-189
    • Lee, S.1    Tanaka, T.2    Anzai, K.3    Kirino, Y.4    Aoyagi, H.5    Sugihara, G.6
  • 10
    • 0015499206 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin a I. Studies of the unit conductance channel
    • Hladky, S.B. and Haydon, D.A. (1972) Ion transfer across lipid membranes in the presence of gramicidin A I. Studies of the unit conductance channel. Biochim. Biophys. Acta 274, 294-312
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 11
    • 0015513556 scopus 로고
    • The unit conductance channel of alamethicin
    • Gordon, L.G.M. and Haydon, D.A. (1972) The unit conductance channel of alamethicin. Biochim. Biophys. Acta 255, 1014-1018
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 1014-1018
    • Gordon, L.G.M.1    Haydon, D.A.2
  • 12
    • 0019852408 scopus 로고
    • Mellitin forms channels in lipid bilayers
    • Tosteson, M.T. and Tosteson, D.C. (1981) Mellitin forms channels in lipid bilayers. Biophys. J. 36, 109-116
    • (1981) Biophys. J. , vol.36 , pp. 109-116
    • Tosteson, M.T.1    Tosteson, D.C.2
  • 13
    • 0019721485 scopus 로고
    • The effect of mastoparan on ion movement in black lipid membrane
    • Okamura, K., Inui, K., Hirai, Y., and Nakajima, T. (1981) The effect of mastoparan on ion movement in black lipid membrane. Biomed. Res. 2, 450-452
    • (1981) Biomed. Res. , vol.2 , pp. 450-452
    • Okamura, K.1    Inui, K.2    Hirai, Y.3    Nakajima, T.4
  • 15
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., Fink, J., Merrifield, R.B., and Mauzerall, D. (1988) Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA 85, 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
  • 16
    • 0024438756 scopus 로고
    • Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
    • Duclohier, H., Molle, G., and Sach, G. (1989) Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56, 1017-1021
    • (1989) Biophys. J. , vol.56 , pp. 1017-1021
    • Duclohier, H.1    Molle, G.2    Sach, G.3
  • 18
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar bilayer membranes
    • Kagan, B.L., Selsted, M.E., Ganz, T., and Lehrer, R.I. (1990) Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar bilayer membranes. Proc. Natl. Acad. Sci. USA 87, 210-214
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 19
    • 0018236743 scopus 로고
    • Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes
    • Schein, S.J., Kagan, B.L., and Finkelstein, A. (1978) Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature 276, 159-163
    • (1978) Nature , vol.276 , pp. 159-163
    • Schein, S.J.1    Kagan, B.L.2    Finkelstein, A.3
  • 20
    • 0020560941 scopus 로고
    • Mode of action of yeast killer toxins: Channel formation in lipid bilayer membranes
    • Kagan, B.L. (1983) Mode of action of yeast killer toxins: channel formation in lipid bilayer membranes. Nature 302, 709-711
    • (1983) Nature , vol.302 , pp. 709-711
    • Kagan, B.L.1
  • 21
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved on insect immunity
    • Steiner, H., Hultmark, D., Engstrom, A., Bennich, H., and Boman, H.G. (1981) Sequence and specificity of two antibacterial proteins involved on insect immunity. Nature 292, 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 22
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449-5453
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 23
    • 0025787585 scopus 로고
    • Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibial skin
    • Mor, A., Nguyen, V.H., Delfour, A., Migliore-Samour, D., and Nicolas, P. (1991) Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibial skin. Biochemistry 30, 8824-8830
    • (1991) Biochemistry , vol.30 , pp. 8824-8830
    • Mor, A.1    Nguyen, V.H.2    Delfour, A.3    Migliore-Samour, D.4    Nicolas, P.5
  • 24
    • 0010326104 scopus 로고
    • Improvements in the method of determining individual phospholipids in a complex mixture by successive chemical hydrolyses
    • Dawson, R.M.C., Hemington, N., and Davenport, J.B. (1962) Improvements in the method of determining individual phospholipids in a complex mixture by successive chemical hydrolyses. Biochem. J. 84, 497-501
    • (1962) Biochem. J. , vol.84 , pp. 497-501
    • Dawson, R.M.C.1    Hemington, N.2    Davenport, J.B.3
  • 25
    • 0014899296 scopus 로고
    • Precise quantitative determination of human blood lipids by thin-lay er and triethylaminoethyl-cellulose column chromatography
    • Turner, J.D. and Rouser, G. (1970) Precise quantitative determination of human blood lipids by thin-lay er and triethylaminoethyl-cellulose column chromatography. Anal. Biochem. 38, 423-436
    • (1970) Anal. Biochem. , vol.38 , pp. 423-436
    • Turner, J.D.1    Rouser, G.2
  • 26
    • 0015821003 scopus 로고
    • The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
    • Verkleij, A.J., Zwaal, R.F.A., Roelofsen, B., Comfurius, P., Kastelijn, D., and van Deenen, L.L.M. (1973) The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta 323, 178-193
    • (1973) Biochim. Biophys. Acta , 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
  • 27
    • 0014262615 scopus 로고
    • Lipids of Salmonella typhimurium and Escherichia coli: Structure and metabolism
    • Ames, G.F. (1968) Lipids of Salmonella typhimurium and Escherichia coli: Structure and metabolism. J. Bacteriol. 95, 833-843
    • (1968) J. Bacteriol. , vol.95 , pp. 833-843
    • Ames, G.F.1
  • 28
    • 0015505380 scopus 로고
    • Metabolism and function of the membrane phospholipids of Escherichia coli
    • Cronan, J.E. and Roy-Vagelos, P. (1972) Metabolism and function of the membrane phospholipids of Escherichia coli. Biochim. Biophys. Acta 265, 25-60
    • (1972) Biochim. Biophys. Acta , vol.265 , pp. 25-60
    • Cronan, J.E.1    Roy-Vagelos, P.2
  • 30
    • 0018796271 scopus 로고
    • Proton electrochemical gradient in Escherichia coli cells and its relation to active transport of lactose
    • Zilberstein, D., Schuldiner, S., and Radan, E. (1979) Proton electrochemical gradient in Escherichia coli cells and its relation to active transport of lactose. Biochemistry 18, 669-673
    • (1979) Biochemistry , vol.18 , pp. 669-673
    • Zilberstein, D.1    Schuldiner, S.2    Radan, E.3
  • 31
    • 0010687584 scopus 로고
    • A methodological approach
    • (Ellory, J.C. and Young, J.D., eds.), Academic Press, London
    • Rink, T.J. and Hladky, S.B. (1982) A methodological approach in Red Cell Membrane (Ellory, J.C. and Young, J.D., eds.) pp. 321-334, Academic Press, London
    • (1982) Red Cell Membrane , pp. 321-334
    • Rink, T.J.1    Hladky, S.B.2
  • 32
    • 0024551246 scopus 로고
    • Basic amphipathic helical peptides induce destabilization and fusion of acidic and neutral liposomes
    • Suenaga, M., Lee, S., Park, N.G., Aoyagi, H., Kato, T., Umeda, A., and Amako, K. (1989) Basic amphipathic helical peptides induce destabilization and fusion of acidic and neutral liposomes. Biochim. Biophys. Acta 981, 143-150
    • (1989) Biochim. Biophys. Acta , vol.981 , pp. 143-150
    • Suenaga, M.1    Lee, S.2    Park, N.G.3    Aoyagi, H.4    Kato, T.5    Umeda, A.6    Amako, K.7
  • 34
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electric properties
    • Montal, M. and Mueller, P. (1972) Formation of bimolecular membranes from lipid monolayers and a study of their electric properties. Proc. Natl. Acad. Sci. USA 69, 3561-3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 35
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • Cociancich, S., Ghazi, A., Hetru, C., Hoffmann, J.A., and Letellier, L. (1993) Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268, 19239-19245
    • (1993) J. Biol. Chem. , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 36
    • 51249190004 scopus 로고
    • Curvilinear regression course of human brain lipid composition changes with age
    • Rouser, G. and Yamamoto, Y. (1968) Curvilinear regression course of human brain lipid composition changes with age. Lipids 3, 284-287
    • (1968) Lipids , vol.3 , pp. 284-287
    • Rouser, G.1    Yamamoto, Y.2
  • 37
    • 0014603132 scopus 로고
    • Species variations in phospholipid class distribution of organs: II. Heart and skeletal muscle
    • Simon, G. and Rouser, G. (1969) Species variations in phospholipid class distribution of organs: II. Heart and skeletal muscle. Lipids 4, 607-614
    • (1969) Lipids , vol.4 , pp. 607-614
    • Simon, G.1    Rouser, G.2
  • 38
    • 0014601237 scopus 로고
    • Species variations in phospholipid class distribution of organs: I. Kidney, liver and spleen
    • Rouser, G., Simon, G., and Kritchevsky, G. (1969) Species variations in phospholipid class distribution of organs: I. Kidney, liver and spleen. Lipids 4, 599-606
    • (1969) Lipids , vol.4 , pp. 599-606
    • Rouser, G.1    Simon, G.2    Kritchevsky, G.3
  • 39
    • 0014517722 scopus 로고
    • Variations among vertebrates of lung phospholipid class composition
    • Baxter, C.F., Rouser, G., and Simon, G. (1969) Variations among vertebrates of lung phospholipid class composition. Lipids 4, 243-244
    • (1969) Lipids , vol.4 , pp. 243-244
    • Baxter, C.F.1    Rouser, G.2    Simon, G.3
  • 40
    • 0014779037 scopus 로고
    • Phospholipid content of human and guinea pig muscle: Post-mortem changes and variations with muscle composition
    • Hof, H. and Simon, R.G. (1970) Phospholipid content of human and guinea pig muscle: Post-mortem changes and variations with muscle composition. Lipids 5, 485-487
    • (1970) Lipids , vol.5 , pp. 485-487
    • Hof, H.1    Simon, R.G.2
  • 41
    • 0014514481 scopus 로고
    • Changes in the phospholipid composition of human aorta with age
    • Rouser, G. and Solomon, R.D. (1969) Changes in the phospholipid composition of human aorta with age. Lipids 4, 232-234
    • (1969) Lipids , vol.4 , pp. 232-234
    • Rouser, G.1    Solomon, R.D.2
  • 42
    • 0014448632 scopus 로고
    • Lipid composition of subcellular particles of human blood platelets
    • Marcus, A.J., Ullman, H.L., and Safier, L.B. (1969) Lipid composition of subcellular particles of human blood platelets. J. Lipid Res. 10, 108-114
    • (1969) J. Lipid Res. , vol.10 , pp. 108-114
    • Marcus, A.J.1    Ullman, H.L.2    Safier, L.B.3
  • 43
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • Boheim, G. (1974) Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol. 19, 277-303
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 44
    • 0023491341 scopus 로고
    • Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin
    • Sahl, H.-G., Kordel, M., and Benz, R. (1987) Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch. Microbiol. 149, 120-124
    • (1987) Arch. Microbiol. , vol.149 , pp. 120-124
    • Sahl, H.-G.1    Kordel, M.2    Benz, R.3
  • 45
    • 0021272091 scopus 로고
    • Studies on the mechanism of action of channel-forming colicins using artificial membranes
    • Davison, V.L., Brumen, K.R., Cramer, W.A., and Cohen, F.S. (1984) Studies on the mechanism of action of channel-forming colicins using artificial membranes. J. Membr. Biol. 79, 105-118
    • (1984) J. Membr. Biol. , vol.79 , pp. 105-118
    • Davison, V.L.1    Brumen, K.R.2    Cramer, W.A.3    Cohen, F.S.4
  • 46
    • 0023688987 scopus 로고
    • Properties of ion channels formed by Staphylococcus aureus δ-toxin
    • Mellor, I.R., Thomas, D.H., and Sansom, M.S.P. (1988) Properties of ion channels formed by Staphylococcus aureus δ-toxin. Biochim. Biophys. Acta 942, 280-294
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 280-294
    • Mellor, I.R.1    Thomas, D.H.2    Sansom, M.S.P.3
  • 47
    • 0023858915 scopus 로고
    • Mode of action of the staphylococcinlike peptide Pep 5: Voltage-dependent depolarization of bacterial and artificial membranes
    • Kordel, M., Benz, R., and Sahl, H.-G. (1988) Mode of action of the staphylococcinlike peptide Pep 5: Voltage-dependent depolarization of bacterial and artificial membranes. J. Bacteriol. 170, 84-88
    • (1988) J. Bacteriol. , vol.170 , pp. 84-88
    • Kordel, M.1    Benz, R.2    Sahl, H.-G.3
  • 50
    • 0025977855 scopus 로고
    • Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers
    • Matsuzaki, K., Harada, M., Funakoshi, S., Fujii, N., and Miyajima, K. (1991) Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta 1063, 162-170
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 162-170
    • Matsuzaki, K.1    Harada, M.2    Funakoshi, S.3    Fujii, N.4    Miyajima, K.5
  • 51
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, Magainin 2
    • Matsuzaki, K., Sugishita, K., Fujii, N., and Miyajima, K. (1995) Molecular basis for membrane selectivity of an antimicrobial peptide, Magainin 2. Biochemistry 34, 3423-3429
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 52
    • 0016163537 scopus 로고
    • Dual mechanism for the action of cholesterol on membrane permeability
    • Szabo, G. (1974) Dual mechanism for the action of cholesterol on membrane permeability. Nature 252, 47-49
    • (1974) Nature , vol.252 , pp. 47-49
    • Szabo, G.1
  • 53
    • 0027202188 scopus 로고
    • Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP
    • Guihard, G., Benedetti, H., Besnard, M., and Letellier, L. (1993) Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP. J. Biol. Chem. 268, 17775-17780
    • (1993) J. Biol. Chem. , vol.268 , pp. 17775-17780
    • Guihard, G.1    Benedetti, H.2    Besnard, M.3    Letellier, L.4


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