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Volumn 2, Issue , 2012, Pages

Neutron diffraction studies of the interaction between amphotericin B and lipid-sterol model membranes

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOTERICIN B; CHOLESTEROL; ERGOSTEROL; LIPID; MEMBRANE LIPID; STEROL;

EID: 84868271598     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00778     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 33745646085 scopus 로고    scopus 로고
    • Invasive fungal infections: A review of epidemiology and management options
    • DOI 10.1099/jmm.0.46548-0
    • Enoch, D.A., Ludlam, H. A. & Brown, N. M.Invasive fungal infections: areview of epidemiology and management options. J Med. Microbiol. 55, 809-818 (2006). (Pubitemid 43974685)
    • (2006) Journal of Medical Microbiology , vol.55 , Issue.7 , pp. 809-818
    • Enoch, D.A.1    Ludlam, H.A.2    Brown, N.M.3
  • 2
    • 33847114442 scopus 로고    scopus 로고
    • Trends in the epidemiology of invasive fungal infections
    • Warnock, D. W. Trends in the epidemiology of invasive fungal infections. J. Med. Mycol. 48, 809-818 (2007).
    • (2007) J. Med. Mycol. , vol.48 , pp. 809-818
    • Warnock, D.W.1
  • 3
    • 63849233258 scopus 로고    scopus 로고
    • The changing face of epidemiology of invasive fungal disease in Europe
    • Lass-Flo, C. The changing face of epidemiology of invasive fungal disease in Europe. Mycoses 52, 197-205 (2009).
    • (2009) Mycoses , vol.52 , pp. 197-205
    • Lass-Flo, C.1
  • 4
    • 0031969879 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular factors that contribute to antifungal drug resistance
    • White, T. C., Marr, K. A. & Bowden, R. A. Clinical, cellular, and molecular factors that contribute to antifungal drug resistance. Clinical Microbiol. Rev. 11, 382-402 (1998). (Pubitemid 28197359)
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.2 , pp. 382-402
    • White, T.C.1    Marr, K.A.2    Bowden, R.A.3
  • 5
    • 84855683118 scopus 로고    scopus 로고
    • Antifungal resistance and new strategies to control fungal infections
    • Article ID 713687
    • Vandeputte, P., Ferrari, S. & Coste, A. T. Antifungal resistance and new strategies to control fungal infections. Int. J. Microbiol. 2012, Article ID 713687 (2012).
    • (2012) Int. J. Microbiol.
    • Vandeputte, P.1    Ferrari, S.2    Coste, A.T.3
  • 6
    • 84055199809 scopus 로고    scopus 로고
    • Antifungal drug resistance: Mechanisms, epidemiology, and consequences for treatment
    • Pfaller, M. A. Antifungal drug resistance: mechanisms, epidemiology, and consequences for treatment. Am. J. Med. 125 (Suppl 1), S3-S13 (2012).
    • (2012) Am. J. Med. , vol.125 , Issue.SUPPL. 1
    • Pfaller, M.A.1
  • 7
    • 84862060971 scopus 로고    scopus 로고
    • Detection of amphotericin B resistance in Candida haemulonii and closely related species by use of the Etest, Vitek-2 yeast susceptibility system, and CLSI and EUCAST broth microdilution methods
    • Shin, J. H. et al. Detection of amphotericin B resistance in Candida haemulonii and closely related species by use of the Etest, Vitek-2 yeast susceptibility system, and CLSI and EUCAST broth microdilution methods. J Clinical Microbiol. 50, 1852-5 (2012).
    • (2012) J Clinical Microbiol. , vol.50 , pp. 1852-1855
    • Shin, J.H.1
  • 8
    • 0033026744 scopus 로고    scopus 로고
    • In vitro amphotericin B resistance in clinical isolates of Aspergillus terreus, with a head-to-head comparison to voriconazole
    • Sutton, D. A. et al. In vitro amphotericin B resistance in clinical isolates of Aspergillus terreus, with a head-to-head comparison to voriconazole. J. Clinical Microbiol. 37, 2343-2345 (1999). (Pubitemid 29277804)
    • (1999) Journal of Clinical Microbiology , vol.37 , Issue.7 , pp. 2343-2345
    • Sutton, D.A.1    Sanche, S.E.2    Revankar, S.G.3    Fothergill, A.W.4    Rinaldi, M.G.5
  • 9
    • 84868270806 scopus 로고    scopus 로고
    • Amphotericin B resistance is associated with fatal Aspergillus flavus infection
    • Hadrich, I. et al. Amphotericin B resistance is associated with fatal Aspergillus flavus infection. Medical Mycology 2012, EPUB 1-6 (2012).
    • (2012) Medical Mycology , vol.2012 , pp. 1-6
    • Hadrich, I.1
  • 11
    • 0036177169 scopus 로고    scopus 로고
    • Amphotericin B nephrotoxicity
    • Deray, G. Amphotericin B nephrotoxicity. J. Antimicr. Chemother. 49 (Suppl. S1), 37-41 (2002). (Pubitemid 34162655)
    • (2002) Journal of Antimicrobial Chemotherapy , vol.49 , Issue.SUPPL. S1 , pp. 37-41
    • Deray, G.1
  • 12
    • 0015823874 scopus 로고
    • Aqueous pores created in thin lipid membranes by the polyene antibiotics nystatin and amphotericin B
    • Finkelstein, A. & Holz, R. Aqueous pores created in thin lipid membranes by the polyene antibiotics nystatin and amphotericin B. Membranes 2, 377-348 (1973).
    • (1973) Membranes , vol.2 , pp. 377-348
    • Finkelstein, A.1    Holz, R.2
  • 13
    • 0015668370 scopus 로고
    • Selective membrane toxicity of the polyene antibiotics: Studies on lecithin model membranes (liposomes)
    • Hsuchen, C.-C. & Feingold, D. S. Selective membrane toxicity of the polyene antibiotics: studies on lecithin model membranes (liposomes). Antimicrob. Agents Chemother. 4, 309-315 (1973).
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 309-315
    • Hsuchen, C.-C.1    Feingold, D.S.2
  • 14
    • 0016670377 scopus 로고
    • Pores formed by nystatin. differences in its one-side and two-side action
    • Marty, A. & Finkelstein, A. Pores formed by nystatin. differences in its one-side and two-side action. J. Gen. Physiol. 65, 515-526 (1975).
    • (1975) J. Gen. Physiol. , vol.65 , pp. 515-526
    • Marty, A.1    Finkelstein, A.2
  • 15
    • 0026777510 scopus 로고
    • A sequential mechanism for the formation of aqueous channels by amphotericin-B in liposomes-The effect of sterols and phospholipid-composition Biochim
    • Cohen, B. E. A sequential mechanism for the formation of aqueous channels by amphotericin-B in liposomes-the effect of sterols and phospholipid- composition, Biochim. Biophys. Acta-Biomembranes 1108, 49-58 (1992).
    • (1992) Biophys. Acta-Biomembranes , vol.1108 , pp. 49-58
    • Cohen, B.E.1
  • 16
    • 0032532193 scopus 로고    scopus 로고
    • On the role of sterol in the formation of the amphotericin B channel
    • DOI 10.1016/S0005-2736(98)00134-5, PII S0005273698001345
    • Cotero, B. V., Rebolledo-Antunez, S. & Ortega-Blake, I. On the role of sterol in the formation ofthe amphotericinBchannel. Biochim. Biophys. Acta-Biomembranes 1375, 43-51 (1998). (Pubitemid 28514428)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1375 , Issue.1-2 , pp. 43-51
    • Cotero, B.V.1    Rebolledo-Antunez, S.2    Ortega-Blake, I.3
  • 17
    • 0141642130 scopus 로고    scopus 로고
    • Amphotericin B channels in the bacterial membrane: Role of sterol and temperature
    • Venegas, B., González-Damián, J., Celis, H. & Ortega-Blake, I. Amphotericin B channels in the bacterial membrane: role of sterol and temperature. Biophys. J. 85, 2323-2332 (2003). (Pubitemid 37210782)
    • (2003) Biophysical Journal , vol.85 , Issue.4 , pp. 2323-2332
    • Venegas, B.1    Gonzalez-Damian, J.2    Celis, H.3    Ortega-Blake, I.4
  • 18
    • 0000171794 scopus 로고    scopus 로고
    • Role of the sterol superlattice in the partitioning of the antifungal drug nystatin into lipid membranes
    • DOI 10.1021/bi980290k
    • Wang, M. M., Sugar, I. P. & Chong, P. L. G. Role of the sterol superlattice in the partitioning of the antifungal drug nystatin into lipid membranes. Biochem. 37, 11797-11805 (1998). (Pubitemid 28400051)
    • (1998) Biochemistry , vol.37 , Issue.34 , pp. 11797-11805
    • Wang, M.M.1    Sugar, I.P.2    Chong, P.L.-G.3
  • 19
    • 84857134391 scopus 로고    scopus 로고
    • Amphotericin primarily kills yeast by simply binding ergosterol
    • Gray, K. C. et al. Amphotericin primarily kills yeast by simply binding ergosterol. Proc. Natl. Acad. Sci. (U.S.A) 109, 2234-2239 (2012).
    • (2012) Proc. Natl. Acad. Sci. (U.S.A) , vol.109 , pp. 2234-2239
    • Gray, K.C.1
  • 20
    • 79954733379 scopus 로고
    • Small angle neutron scattering studies of the effects of amphotericin B on phospholipid and phospholipid-sterol membrane structure
    • Foglia, F. F. et al. Small angle neutron scattering studies of the effects of amphotericin B on phospholipid and phospholipid-sterol membrane structure. Biochim. Biophys. Acta-Biomembranes 1808, 1574-1580 (2010).
    • (1808) Biochim. Biophys. Acta-Biomembranes , pp. 1574-1580
    • Foglia, F.F.1
  • 22
    • 33747791267 scopus 로고    scopus 로고
    • Interaction between nystatin and natural membrane lipids in Langmuir monolayers-The role of a phospholipid in the mechanism of polyenes' mode of action
    • Katarzyna, H. W. & Patrycja, D. L. Interaction between nystatin and natural membrane lipids in Langmuir monolayers-The role of a phospholipid in the mechanism of polyenes' mode of action. Biophys. Chem. 123, 154-161 (2006).
    • (2006) Biophys. Chem. , vol.123 , pp. 154-161
    • Katarzyna, H.W.1    Patrycja, D.L.2
  • 24
    • 34249336707 scopus 로고    scopus 로고
    • Effect of antibiotic amphotericin B on structural and dynamic properties of lipid membranes formed with egg yolk phosphatidylcholine
    • DOI 10.1016/j.chemphyslip.2007.03.007, PII S0009308407000485
    • Herec, M., Islamov, A., Kuklin, A., Gagoś, M. & Gruszecki, W. I. Effect of antibiotic amphotericin B on structural and dynamic properties of lipid membranes formed with egg yolk phosphatidylcholine. Chem. Phys. Lipids 147, 78-86 (2007). (Pubitemid 46818168)
    • (2007) Chemistry and Physics of Lipids , vol.147 , Issue.2 , pp. 78-86
    • Herec, M.1    Islamov, A.2    Kuklin, A.3    Gagos, M.4    Gruszecki, W.I.5
  • 25
    • 28544446205 scopus 로고    scopus 로고
    • Binding of antibiotic amphotericin B to lipid membranes: Monomolecular layer technique and linear dichroism-FTIR studies
    • DOI 10.1080/09687860500287832
    • Gagoś, M., Gabrielska, J., Dalla Serra, M. & Gruszecki, W. I. Binding of antibiotic amphotericin B to lipid membranes: monomolecular layer technique and linear dichroism-FTIR studies. Mol. Membrane Biol. 22, 433-442 (2005). (Pubitemid 41747105)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.5 , pp. 433-442
    • Gagos, M.1    Gabrielska, J.2    Dalla Serra, M.3    Gruszecki, W.I.4
  • 26
    • 0018152154 scopus 로고
    • Effect of amphotericin on cholesterol-containing liposomes of egg phosphatidylcholine and didocosenoyl phosphatidylcholine
    • van Hoogevest, P. & de Kruijff, B. Effect of amphotericin on cholesterol-containing liposomes of egg phosphatidylcholine and didocosenoyl phosphatidylcholine. Biochim. Biophys. Acat-Biomembranes 511, 397-407 (1978).
    • (1978) Biochim. Biophys. Acat-Biomembranes , vol.511 , pp. 397-407
    • Van Hoogevest, P.1    De Kruijff, B.2
  • 27
    • 23044484361 scopus 로고    scopus 로고
    • Mycosamine orientation of amphotericin B controlling interaction with ergosterol: Sterol-dependent activity of conformation-restricted derivatives with an amino-carbonyl bridge
    • DOI 10.1021/ja051597r
    • Matsumori, N., Sawada, Y. & Murata, M. Mycosamine Orientation of amphotericin B controlling interaction with ergosterol: sterol-dependent activity of conformation-restricted derivatives with an amino-carbonyl bridge. J. Am. Chem. Soc. 127, 10667-10675 (2005). (Pubitemid 41061440)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.30 , pp. 10667-10675
    • Matsumori, N.1    Sawada, Y.2    Murata, M.3
  • 28
    • 70449111481 scopus 로고    scopus 로고
    • Mechanical properties of interacting lipopolysaccharide membranes from bacteria mutants studied by specular and off-specular neutron scattering
    • Schneck, E. et al. Mechanical properties of interacting lipopolysaccharide membranes from bacteria mutants studied by specular and off-specular neutron scattering. Phys. Rev. E 80, 041929/1 (2009).
    • (2009) Phys. Rev. e , vol.80
    • Schneck, E.1
  • 30
    • 0036923942 scopus 로고    scopus 로고
    • Structure of gel phase DMPC determined by x-ray diffraction
    • Tristram-Nagle, S., Liu, Y., Legleiter, J. & Nagle, J. F. Structure of gel pahse DMPC determined by X-ray diffraction. Biophys. J. 83, 3324-3335 (2002). (Pubitemid 36041950)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3324-3335
    • Tristram-Nagle, S.1    Liu, Y.2    Legleiter, J.3    Nagle, J.F.4
  • 31
    • 0018597218 scopus 로고
    • The structure of lipid bilayers and the effects of general anaesthetics. An x-ray and neutron diffraction study
    • DOI 10.1016/0022-2836(79)90403-0
    • Franks, N. P. & Lieb, W. R. Structures of lipid bilayers and the effects of general anaesthetics: X-ray and neutron diffraction study. J. Mol. Biol. 133, 469-500 (1979). (Pubitemid 10157903)
    • (1979) Journal of Molecular Biology , vol.133 , Issue.4 , pp. 469-500
    • Franks, N.P.1    Lieb, W.R.2
  • 32
    • 60849122588 scopus 로고    scopus 로고
    • Viewing the bilayer hydrophobic core using neutron diffraction
    • Han, X. & Hirstova, K. Viewing the bilayer hydrophobic core using neutron diffraction. J. Membrane Biol. 227, 123-131 (2009).
    • (2009) J. Membrane Biol. , vol.227 , pp. 123-131
    • Han, X.1    Hirstova, K.2
  • 33
    • 84868280506 scopus 로고    scopus 로고
    • www.ncnr.nist.gov/instruments/bt1/neutron.html
  • 34
    • 0020824652 scopus 로고
    • Neutron diffraction analysis of cytochrom b5 reconstituted in deuterated lipid bilayers
    • Gogol, E. P., Engelman, D. M. & Zaccai, G. Neutron diffraction analysis of cytochrom b5 reconstituted in deuterated lipid bilayers. Biophys. J. 43, 285-292 (1983).
    • (1983) Biophys. J. , vol.43 , pp. 285-292
    • Gogol, E.P.1    Engelman, D.M.2    Zaccai, G.3
  • 35
    • 0016633210 scopus 로고
    • Neutron diffraction studies on location of water in lecithin bilayer model membranes
    • Zaccai, G., Blasie, J. K. & Schoenborn, B. P. Neutron diffraction studies on location of water in lecithin bilayer model membranes. Proc. Natl. Acad. Sci. (USA) 72, 376-380 (1975).
    • (1975) Proc. Natl. Acad. Sci. (USA) , vol.72 , pp. 376-380
    • Zaccai, G.1    Blasie, J.K.2    Schoenborn, B.P.3
  • 36
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • DOI 10.1021/bi00434a042
    • Jacobs, R. E. & White, S. H. The nature of the hydrophobic binding of small peptides at the bilayer interface-implications for the insertion of transbilayer helices. Biochem. 28, 3421-3437 (1989). (Pubitemid 19121937)
    • (1989) Biochemistry , vol.28 , Issue.8 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 37
    • 0017232478 scopus 로고
    • Structural analysis of hydrated egg lecithin and cholesterol bilayers 2
    • Worcester, D. L. & Frank, N. P. Structural analysis of hydrated egg lecithin and cholesterol bilayers 2. Neutron diffraction. J. Mol. Biol. 100, 359-378 (1976).
    • (1976) Neutron Diffraction. J. Mol. Biol. , vol.100 , pp. 359-378
    • Worcester, D.L.1    Frank, N.P.2


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