메뉴 건너뛰기




Volumn 1667, Issue 1, 2004, Pages 91-100

Membrane-permeabilizing activities of amphidinol 3, polyene-polyhydroxy antifungal from a marine dinoflagellate

Author keywords

Amphidinium klebsii; Amphidinol; Amphotericin B

Indexed keywords

AMPHIDINOL 3; AMPHOTERICIN B; ANTIFUNGAL AGENT; CHOLESTEROL; DETERGENT; ERGOSTEROL; FILIPIN; LIPOSOME; POLYENE; POLYENE ANTIBIOTIC AGENT; TRITON X 100; UNCLASSIFIED DRUG;

EID: 7744220153     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.09.002     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 0001377493 scopus 로고
    • Microalgal metabolites
    • Y. Shimizu Microalgal metabolites Chem. Rev. 5 1993 1685 1698
    • (1993) Chem. Rev. , vol.5 , pp. 1685-1698
    • Shimizu, Y.1
  • 3
    • 0026322293 scopus 로고
    • Amphidinol, a polyhydroxy-polyene antifungal agent with an unprecedented structure, from a marine dinoflagellate, Amphidinium klebsii
    • M. Satake, M. Murata, M. Yasumoto, T. Fujita, and H. Naoki Amphidinol, a polyhydroxy-polyene antifungal agent with an unprecedented structure, from a marine dinoflagellate, Amphidinium klebsii J. Am. Chem. Soc. 113 1991 9859 9861
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9859-9861
    • Satake, M.1    Murata, M.2    Yasumoto, M.3    Fujita, T.4    Naoki, H.5
  • 4
    • 0001569209 scopus 로고    scopus 로고
    • Chemical structures of amphidinols 5 and 6 isolated from marine dinoflagellate Amphidinium klebsii and their cholesterol-dependent membrane disruption
    • G.K. Paul, N. Matsumori, K. Konoki, M. Murata, and K. Tachibana Chemical structures of amphidinols 5 and 6 isolated from marine dinoflagellate Amphidinium klebsii and their cholesterol-dependent membrane disruption J. Mar. Biotechnol. 5 1997 124 128
    • (1997) J. Mar. Biotechnol. , vol.5 , pp. 124-128
    • Paul, G.K.1    Matsumori, N.2    Konoki, K.3    Murata, M.4    Tachibana, K.5
  • 5
    • 0029153948 scopus 로고
    • Isolation and chemical structure of amphidinol 2, a potent hemolytic compound from marine dinoflagellate Amphidinium klebsii
    • G.K. Paul, N. Matsumori, M. Murata, and K. Tachibana Isolation and chemical structure of amphidinol 2, a potent hemolytic compound from marine dinoflagellate Amphidinium klebsii Tetrahedron Lett. 36 1995 6279 6282
    • (1995) Tetrahedron Lett. , vol.36 , pp. 6279-6282
    • Paul, G.K.1    Matsumori, N.2    Murata, M.3    Tachibana, K.4
  • 6
    • 0004605946 scopus 로고    scopus 로고
    • Structure of amphidinol 3 and its cholesterol-dependent membrane perturbation: A strong antifungal metabolites produced by dinoflagellate, Amphidinium klebsii
    • T. Yasumoto Y. Oshima Y. Fukuyo Intergovernmental Oceanographic Commission of UNESCO Sendai
    • G.K. Paul, N. Matsumori, K. Konoki, M. Sasaki, M. Murata, and K. Tachibana Structure of amphidinol 3 and its cholesterol-dependent membrane perturbation: a strong antifungal metabolites produced by dinoflagellate, Amphidinium klebsii T. Yasumoto Y. Oshima Y. Fukuyo Harmful and Toxic Algal Blooms 1996 Intergovernmental Oceanographic Commission of UNESCO Sendai 503 506
    • (1996) Harmful and Toxic Algal Blooms , pp. 503-506
    • Paul, G.K.1    Matsumori, N.2    Konoki, K.3    Sasaki, M.4    Murata, M.5    Tachibana, K.6
  • 7
    • 0033518615 scopus 로고    scopus 로고
    • Absolute configuration of amphidinol 3, the first complete structure determined from amphidinol homologues: Application of a new configuration analysis based on carbon-hydrogen spin-coupling constants
    • M. Murata, S. Matsuoka, N. Matsumori, G.K. Paul, and K. Tachibana Absolute configuration of amphidinol 3, the first complete structure determined from amphidinol homologues: application of a new configuration analysis based on carbon-hydrogen spin-coupling constants J. Am. Chem. Soc. 121 1999 870 871
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 870-871
    • Murata, M.1    Matsuoka, S.2    Matsumori, N.3    Paul, G.K.4    Tachibana, K.5
  • 9
    • 0036225153 scopus 로고    scopus 로고
    • The mechanism of the hemolytic activity of polyene antibiotics
    • A. Knopik-Skrocka, and J. Bielawski The mechanism of the hemolytic activity of polyene antibiotics Cell. Mol. Biol. Lett. 7 2002 31 48
    • (2002) Cell. Mol. Biol. Lett. , vol.7 , pp. 31-48
    • Knopik-Skrocka, A.1    Bielawski, J.2
  • 11
    • 0015980909 scopus 로고
    • Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes: III. Molecular structure of the polyene antibiotic-cholesterol complexes
    • B. De Kruijff, and R.A. Demel Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes: III. Molecular structure of the polyene antibiotic-cholesterol complexes Biochim. Biophys. Acta 339 1974 57 70
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 57-70
    • De Kruijff, B.1    Demel, R.A.2
  • 12
    • 0016158807 scopus 로고
    • Structure and function of amphotericin B-cholesterol pores in lipid bilayer membranes
    • T.E. Andreoli Structure and function of amphotericin B-cholesterol pores in lipid bilayer membranes Ann. N.Y. Acad. Sci. 235 1974 448 468
    • (1974) Ann. N.Y. Acad. Sci. , vol.235 , pp. 448-468
    • Andreoli, T.E.1
  • 13
    • 0020068655 scopus 로고
    • Equilibrium binding of amphotericin B and its methyl ester and borate complex to sterols
    • J.D. Readio, and R. Bittman Equilibrium binding of amphotericin B and its methyl ester and borate complex to sterols Biochim. Biophys. Acta 685 1982 219 224 (For example)
    • (1982) Biochim. Biophys. Acta , vol.685 , pp. 219-224
    • Readio, J.D.1    Bittman, R.2
  • 14
    • 0030449320 scopus 로고    scopus 로고
    • Amphotericin B: New life for an old drug
    • S. Hartsel, and J. Bolard Amphotericin B: new life for an old drug Trends Pharmacol. Sci. 17 1996 445 449
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 445-449
    • Hartsel, S.1    Bolard, J.2
  • 15
    • 0037165756 scopus 로고    scopus 로고
    • Amphotericin B covalent dimers forming sterol-dependent ion-permeable membrane channels
    • N. Matsumori, N. Yamaji, S. Matsuoka, T. Oishi, and M. Murata Amphotericin B covalent dimers forming sterol-dependent ion-permeable membrane channels J. Am. Chem. Soc. 124 2002 4180 4181
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4180-4181
    • Matsumori, N.1    Yamaji, N.2    Matsuoka, S.3    Oishi, T.4    Murata, M.5
  • 16
    • 0037071946 scopus 로고    scopus 로고
    • Amphotericin B dimers with bis-amide linkage bearing powerful membrane permeabilizing activity
    • N. Yamaji, N. Matsumori, S. Matsuoka, T. Oishi, and M. Murata Amphotericin B dimers with bis-amide linkage bearing powerful membrane permeabilizing activity Org. Lett. 4 2002 2087 2089
    • (2002) Org. Lett. , vol.4 , pp. 2087-2089
    • Yamaji, N.1    Matsumori, N.2    Matsuoka, S.3    Oishi, T.4    Murata, M.5
  • 17
    • 0344946181 scopus 로고    scopus 로고
    • Amphotericin B-phospholipid covalent conjugates: Dependence of membrane-permeabilizing activitiy on acyl-chain length
    • S. Matsuoka, N. Matsumori, and M. Murata Amphotericin B-phospholipid covalent conjugates: dependence of membrane-permeabilizing activitiy on acyl-chain length M. Org. Biomol. Chem. 1 2003 3882 3884
    • (2003) M. Org. Biomol. Chem. , vol.1 , pp. 3882-3884
    • Matsuoka, S.1    Matsumori, N.2    Murata, M.3
  • 18
    • 2642544178 scopus 로고    scopus 로고
    • An amphotericin B-ergosterol covalent conjugate with powerful membrane permeabilizing activity
    • N. Matsumori, N. Eiraku, S. Matsuoka, T. Oishi, M. Murata, T. Aoki, and T. Ide An amphotericin B-ergosterol covalent conjugate with powerful membrane permeabilizing activity Chem. Biol. 11 2004 673 679
    • (2004) Chem. Biol. , vol.11 , pp. 673-679
    • Matsumori, N.1    Eiraku, N.2    Matsuoka, S.3    Oishi, T.4    Murata, M.5    Aoki, T.6    Ide, T.7
  • 19
    • 0026566087 scopus 로고
    • Permeabilizing action of filipin III on membranes through a filipin-phospholipid binding
    • J. Milhaud Permeabilizing action of filipin III on membranes through a filipin-phospholipid binding Biochim. Biophys. Acta 1105 1992 307 318
    • (1992) Biochim. Biophys. Acta , vol.1105 , pp. 307-318
    • Milhaud, J.1
  • 22
    • 0015126697 scopus 로고
    • Molecular sieving by the Bacillus megaterium cell wall and protoplast
    • R. Scherrer, and P. Gerhardt Molecular sieving by the Bacillus megaterium cell wall and protoplast J. Bacteriol. 107 1971 718 735
    • (1971) J. Bacteriol. , vol.107 , pp. 718-735
    • Scherrer, R.1    Gerhardt, P.2
  • 26
    • 0023802249 scopus 로고
    • A nuclear magnetic resonance study of alamethicin-, δ-haemolysin-, and melittin-induced sodium leakage from large unilamellar vesicles
    • G.F. King, J. Deegan, R. Smith, A. Matouschek, and I.D. Campbell A nuclear magnetic resonance study of alamethicin-, δ-haemolysin-, and melittin-induced sodium leakage from large unilamellar vesicles Biochem. Soc. Trans. 16 1988 594 595
    • (1988) Biochem. Soc. Trans. , vol.16 , pp. 594-595
    • King, G.F.1    Deegan, J.2    Smith, R.3    Matouschek, A.4    Campbell, I.D.5
  • 27
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • A. Helenius, and K. Simons Solubilization of membranes by detergents Biochim. Biophys. Acta 415 1975 29 79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 28
    • 0021111031 scopus 로고
    • Solubilization of phospholipid by detergents structural and kinetic aspects
    • D. Lichtenberg, R.J. Robson, and E.A. Dennis Solubilization of phospholipid by detergents structural and kinetic aspects Biochim. Biophys. Acta 737 1983 285 304
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 285-304
    • Lichtenberg, D.1    Robson, R.J.2    Dennis, E.A.3
  • 30
    • 0015992898 scopus 로고
    • Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin kiposomes: I. Specificity of the membrane permeability changes induced by the polene antibiotics
    • B. De Kruijiff, W.J. Gerritsen, A. Oerlemans, R.A. Demel, and L.L.M. VanDeenen Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin kiposomes: I. Specificity of the membrane permeability changes induced by the polene antibiotics Biochim. Biophys. Acta 339 1974 30 43
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 30-43
    • De Kruijiff, B.1    Gerritsen, W.J.2    Oerlemans, A.3    Demel, R.A.4    Vandeenen, L.L.M.5
  • 31
    • 0030844744 scopus 로고    scopus 로고
    • Molecular properties of amphotericin B membrane channel: A molecular dynamics simulation
    • M. Baginski, H. Resat, and J.A. McCammon Molecular properties of amphotericin B membrane channel: a molecular dynamics simulation Mol. Pharmacol. 52 1997 560 570
    • (1997) Mol. Pharmacol. , vol.52 , pp. 560-570
    • Baginski, M.1    Resat, H.2    McCammon, J.A.3
  • 32
    • 0019483423 scopus 로고
    • Structure of amphotericin B aggregates as revealed by UV and CD spectroscopies
    • C. Ernst, J. Grange, H. Rinnert, G. Dupont, and J. Lematre Structure of amphotericin B aggregates as revealed by UV and CD spectroscopies Biopolymers 20 1981 1575 1588
    • (1981) Biopolymers , vol.20 , pp. 1575-1588
    • Ernst, C.1    Grange, J.2    Rinnert, H.3    Dupont, G.4    Lematre, J.5
  • 33
    • 0030933186 scopus 로고    scopus 로고
    • The formation of amphotericin B ion channels in lipid bilayers
    • G. Fujii, J. Chang, T. Coley, and B. Steere The formation of amphotericin B ion channels in lipid bilayers Biochemistry 36 1997 4959 4968
    • (1997) Biochemistry , vol.36 , pp. 4959-4968
    • Fujii, G.1    Chang, J.2    Coley, T.3    Steere, B.4
  • 34
    • 0018973383 scopus 로고
    • Interaction between phospholipid bilayer membranes and the polyene antibiotic amphotericin B. Lipid state and cholesterol content dependence
    • J. Bolard, M. Seigneuret, and G. Boudet Interaction between phospholipid bilayer membranes and the polyene antibiotic amphotericin B. Lipid state and cholesterol content dependence Biochim. Biophys. Acta 599 1980 280 293
    • (1980) Biochim. Biophys. Acta , vol.599 , pp. 280-293
    • Bolard, J.1    Seigneuret, M.2    Boudet, G.3
  • 35
    • 0020378722 scopus 로고
    • Self-association of some polyene macrolide antibiotics in aqueous media
    • J. Mazerski, J. Bolard, and E. Borowski Self-association of some polyene macrolide antibiotics in aqueous media Biochim. Biophys. Acta 719 1982 11 17
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 11-17
    • Mazerski, J.1    Bolard, J.2    Borowski, E.3
  • 36
    • 0016289086 scopus 로고
    • Cholesterol-phosphatidylcholine interactions in vesicle systems. Implication of vesicle size and proton magnetic resonance line-width changes
    • M.P.N. Gent, and J.H. Prestegard Cholesterol-phosphatidylcholine interactions in vesicle systems. Implication of vesicle size and proton magnetic resonance line-width changes Biochemistry 13 1974 4027 4033
    • (1974) Biochemistry , vol.13 , pp. 4027-4033
    • Gent, M.P.N.1    Prestegard, J.H.2
  • 37
    • 0025993884 scopus 로고
    • Physical properties of the fluid-bilayer component of cell membranes: A perspective
    • M. Bloom, E. Evans, and O.G. Mouritsen Physical properties of the fluid-bilayer component of cell membranes: a perspective Q. Rev. Biophys. 24 1991 293 397
    • (1991) Q. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 38
    • 0033061634 scopus 로고    scopus 로고
    • Control of lipid membrane stability by cholesterol content
    • S. Raffy, and J. Teissie Control of lipid membrane stability by cholesterol content Biophys. J. 76 1999 2076 2080
    • (1999) Biophys. J. , vol.76 , pp. 2076-2080
    • Raffy, S.1    Teissie, J.2
  • 39
    • 0037206162 scopus 로고    scopus 로고
    • Cholesterol markedly reduces ion permeability induced by membrane-bound amphotericin B
    • S. Matsuoka, and M. Murata Cholesterol markedly reduces ion permeability induced by membrane-bound amphotericin B Biochim. Biophys. Acta 1564 2002 429 434
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 429-434
    • Matsuoka, S.1    Murata, M.2
  • 40
    • 0032836561 scopus 로고    scopus 로고
    • Mechansim of hemolysis and erythrocyte transformation caused by lipogrammistin-A, a lipophilic and acylated cyclic polyamine from the skin secretion of soapfishes (Grammistidae)
    • Y. Kobayashi, H. Onuki, and K. Tachibana Mechansim of hemolysis and erythrocyte transformation caused by lipogrammistin-A, a lipophilic and acylated cyclic polyamine from the skin secretion of soapfishes (Grammistidae) Bioorg. Med. Chem. 7 1999 2073 2081
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 2073-2081
    • Kobayashi, Y.1    Onuki, H.2    Tachibana, K.3
  • 42
    • 0017575026 scopus 로고
    • Conjugated polyene fatty acid on fluorescent probes: Spectroscopic characterization
    • L.A. Skalar, B.S. Hudson, M. Petersen, and J. Diamond Conjugated polyene fatty acid on fluorescent probes: spectroscopic characterization Biochemistry 16 1977 813 818
    • (1977) Biochemistry , vol.16 , pp. 813-818
    • Skalar, L.A.1    Hudson, B.S.2    Petersen, M.3    Diamond, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.