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Volumn 1818, Issue 3, 2012, Pages 636-644

Effects of the pore-forming agent nystatin on giant phospholipid vesicles

Author keywords

Giant phospholipid vesicle; Nystatin; Transmembrane pore

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; METHANOL; NYSTATIN; WATER;

EID: 84855753841     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.11.036     Document Type: Article
Times cited : (13)

References (53)
  • 1
    • 0022862167 scopus 로고
    • How do the polyene macrolide antibiotics affect the cellular membrane properties?
    • J. Bolard How do the polyene macrolide antibiotics affect the cellular membrane properties? Biochim. Biophys. Acta 864 1986 257 304
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 257-304
    • Bolard, J.1
  • 2
    • 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
  • 3
    • 0032882718 scopus 로고    scopus 로고
    • Antifungal agents: Mode of action, mechanisms of resistance and correlation of these mechanisms with bacterial resistance
    • M.A. Ghannoum, and L.B. Rice Antifungal agents: mode of action, mechanisms of resistance and correlation of these mechanisms with bacterial resistance Clin. Microbiol. Rev. 12 1999 501 517
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 501-517
    • Ghannoum, M.A.1    Rice, L.B.2
  • 4
    • 0038679668 scopus 로고    scopus 로고
    • Polyene macrolides in clinical practice: Pharmacology and other adverses effects
    • S. Omura, second ed. Academic Press New York
    • C.P. Schaffner Polyene macrolides in clinical practice: pharmacology and other adverses effects S. Omura, Macrolide Antibiotics: Chemistry, Biology and Practice second ed. 2002 Academic Press New York 457 507
    • (2002) Macrolide Antibiotics: Chemistry, Biology and Practice , pp. 457-507
    • Schaffner, C.P.1
  • 5
    • 0032862342 scopus 로고    scopus 로고
    • In-vitro antifungal activity of liposomal nystatin in comparison with nystatin, amphotericin B cholesteryl sulphate, liposomal amphotericin B, amphotericin B lipid complex, amphotericin B desoxycholate, fluconazole and itraconazole
    • A.J. Carrillo-Munoz, G. Quindos, C. Tur, M.T. Ruesga, Y. Miranda, O. del Valle, P.A. Cossum, and T.L. Wallace In-vitro antifungal activity of liposomal nystatin in comparison with nystatin, amphotericin B cholesteryl sulphate, liposomal amphotericin B, amphotericin B lipid complex, amphotericin B desoxycholate, fluconazole and itraconazole J. Antimicrob. Chemother. 44 1999 397 401
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 397-401
    • Carrillo-Munoz, A.J.1    Quindos, G.2    Tur, C.3    Ruesga, M.T.4    Miranda, Y.5    Del Valle, O.6    Cossum, P.A.7    Wallace, T.L.8
  • 6
    • 0036208480 scopus 로고    scopus 로고
    • In vitro activity of nystatin compared with those of liposomal nystatin, amphotericin B and fluconazole against clinical Candida isolates
    • S. Arikan, L. Ostrosky-Zeichner, M. Lozano-Chiu, V. Paetznick, D. Gordon, T. Wallace, and J.H. Rex In vitro activity of nystatin compared with those of liposomal nystatin, amphotericin B and fluconazole against clinical Candida isolates J. Clin. Microbiol. 40 2002 1406 1412
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 1406-1412
    • Arikan, S.1    Ostrosky-Zeichner, L.2    Lozano-Chiu, M.3    Paetznick, V.4    Gordon, D.5    Wallace, T.6    Rex, J.H.7
  • 9
    • 0027136203 scopus 로고
    • How does amphotericin B work? Studies on model membrane systems
    • S.C. Hartsel, C. Hatch, and W. Ayenew How does amphotericin B work? Studies on model membrane systems J. Liposome Res. 3 1993 377 408
    • (1993) J. Liposome Res. , vol.3 , pp. 377-408
    • Hartsel, S.C.1    Hatch, C.2    Ayenew, W.3
  • 10
    • 0038637710 scopus 로고    scopus 로고
    • Cooperative partition model of nystatin interaction with phospholipid vesicles
    • A. Coutinho, and M. Prieto Cooperative partition model of nystatin interaction with phospholipid vesicles Biophys. J. 84 2003 3061 3078
    • (2003) Biophys. J. , vol.84 , pp. 3061-3078
    • Coutinho, A.1    Prieto, M.2
  • 11
    • 0028555787 scopus 로고
    • Nystatin perforated patch recording and its applications to analyses of intracellular mechanisms
    • N. Akaike, and N. Harata Nystatin perforated patch recording and its applications to analyses of intracellular mechanisms Jpn. J. Physiol. 44 1994 433 473
    • (1994) Jpn. J. Physiol. , vol.44 , pp. 433-473
    • Akaike, N.1    Harata, N.2
  • 12
    • 0014471585 scopus 로고
    • The effect of amphotericin B on the water and nonelectrolyte permeability of thin lipid membranes
    • T.E. Andreoli, V.W. Dennis, and A.M. Weigl The effect of amphotericin B on the water and nonelectrolyte permeability of thin lipid membranes J. Gen. Physiol. 53 1969 133 156
    • (1969) J. Gen. Physiol. , vol.53 , pp. 133-156
    • Andreoli, T.E.1    Dennis, V.W.2    Weigl, A.M.3
  • 13
    • 0014822134 scopus 로고
    • The water and nonelectrolyte permeability induced in thin lipid membranes by the polyene antibiotics nystatin and amphotericin B
    • R. Holz, and A. Finkelstein The water and nonelectrolyte permeability induced in thin lipid membranes by the polyene antibiotics nystatin and amphotericin B J. Gen. Physiol. 56 1970 125 145
    • (1970) J. Gen. Physiol. , vol.56 , pp. 125-145
    • Holz, R.1    Finkelstein, A.2
  • 14
    • 6544279184 scopus 로고
    • Protection of fungi against polyene antibiotics by sterols
    • D. Gottlieb, I.I. Carter, J.I.I. Sloneker, and A. Amman Protection of fungi against polyene antibiotics by sterols Science 128 1958 361 365
    • (1958) Science , vol.128 , pp. 361-365
    • Gottlieb, D.1    Carter, I.I.2    Sloneker, J.I.I.3    Amman, A.4
  • 16
    • 33747756395 scopus 로고
    • Effect of polyene antibiotics on protoplast of Neurospora crassa
    • S.C. Kinsky Effect of polyene antibiotics on protoplast of Neurospora crassa J. Bacteriol. 83 1962 351 358
    • (1962) J. Bacteriol. , vol.83 , pp. 351-358
    • Kinsky, S.C.1
  • 17
    • 0014216146 scopus 로고
    • The action of polyene antibiotics on phospholipids-cholesterol structures
    • G. Wiessmann, and G. Sessa The action of polyene antibiotics on phospholipids-cholesterol structures J. Biol. Chem. 42 1967 616 625
    • (1967) J. Biol. Chem. , vol.42 , pp. 616-625
    • Wiessmann, G.1    Sessa, G.2
  • 18
    • 0015800484 scopus 로고
    • Chemistry and biology of polyene macrolide antibiotics
    • J.M.T. Hamilton-Miller Chemistry and biology of polyene macrolide antibiotics Bacteriol. Rev. 37 1973 166 196
    • (1973) Bacteriol. Rev. , vol.37 , pp. 166-196
    • Hamilton-Miller, J.M.T.1
  • 19
    • 0016158807 scopus 로고
    • The structure and function of amphotericin B-cholesterol pores in lipid bilayer membranes
    • T.E. Andreoli The 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
  • 20
    • 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, W.J. Gerritsen, 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    Gerritsen, W.J.2    Demel, R.A.3
  • 21
    • 0018152154 scopus 로고
    • Effect of amphotericin B on cholesterol-containing liposomes of egg phosphatidylcholine and didocoseneoylphosphatidylcholine, A refinement of the model for the formation of pores by amphotericin B in membranes
    • P. van Hoogevest, and B. de Kruijff Effect of amphotericin B on cholesterol-containing liposomes of egg phosphatidylcholine and didocoseneoylphosphatidylcholine, A refinement of the model for the formation of pores by amphotericin B in membranes Biochim. Biophys. Acta 511 1978 397 407
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 397-407
    • Van Hoogevest, P.1    De Kruijff, B.2
  • 22
    • 0015927279 scopus 로고
    • Polyene antibiotic action on lecithin liposomes: Effect of cholesterol and fatty acyl chains
    • C.C. Hsu Chen, and D.S. Feingold Polyene antibiotic action on lecithin liposomes: effect of cholesterol and fatty acyl chains Biochem. Biophys. Res. Commun. 51 1973 972 978
    • (1973) Biochem. Biophys. Res. Commun. , vol.51 , pp. 972-978
    • Hsu Chen, C.C.1    Feingold, D.S.2
  • 23
    • 0016670377 scopus 로고
    • Pores formed in lipid bilayer membranes by nystatin, differences in its one-sided and two-sided action
    • A. Marty, and A. Finkelstein Pores formed in lipid bilayer membranes by nystatin, differences in its one-sided and two-sided action J. Gen. Physiol. 65 1975 515 526
    • (1975) J. Gen. Physiol. , vol.65 , pp. 515-526
    • Marty, A.1    Finkelstein, A.2
  • 24
    • 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
    • K. Ha̧c-Wydro, and P. Dynarowicz-Ła̧tka 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 2006 154 161
    • (2006) Biophys. Chem. , vol.123 , pp. 154-161
    • Ha̧c-Wydro, K.1    Dynarowicz-ŁA̧tka, P.2
  • 25
    • 35148842028 scopus 로고    scopus 로고
    • The influence of phospholipid structure on the interactions with nystatin, a polyene antifungal antibiotic: A Langmuir monolayer study
    • K. Ha̧c-Wydro, J. Kapusta, A. Jagoda, P. Wydro, and P. Dynarowicz-Ła̧tka The influence of phospholipid structure on the interactions with nystatin, a polyene antifungal antibiotic: A Langmuir monolayer study Chem. Phys. Lipids 150 2007 125 135
    • (2007) Chem. Phys. Lipids , vol.150 , pp. 125-135
    • Ha̧c-Wydro, K.1    Kapusta, J.2    Jagoda, A.3    Wydro, P.4    Dynarowicz- Ła̧tka, P.5
  • 26
    • 0020637999 scopus 로고
    • Differences in the interaction of polyene antibiotic amphotericin B with cholesterol or ergosterol-containing phospholipid vesicles, A circular dichroism and permeability study
    • A. Vertut-Croquin, J. Bolard, M. Chabbert, and C. Gary-Bobo Differences in the interaction of polyene antibiotic amphotericin B with cholesterol or ergosterol-containing phospholipid vesicles, A circular dichroism and permeability study Biochemistry 22 1983 2939 2944
    • (1983) Biochemistry , vol.22 , pp. 2939-2944
    • Vertut-Croquin, A.1    Bolard, J.2    Chabbert, M.3    Gary-Bobo, C.4
  • 28
    • 0030933186 scopus 로고    scopus 로고
    • The formation of amphotericin B ion channels in lipid bilayers
    • G. Fujii, J.-E. 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.-E.2    Coley, T.3    Steere, B.4
  • 29
    • 0002596434 scopus 로고    scopus 로고
    • Amphotericin B toxicity and lethality: A tale of two channels
    • B.E. Cohen Amphotericin B toxicity and lethality: a tale of two channels Int. J. Pharm. 162 1998 95 106
    • (1998) Int. J. Pharm. , vol.162 , pp. 95-106
    • Cohen, B.E.1
  • 30
    • 16344382233 scopus 로고    scopus 로고
    • Cholesterol and ergosterol influence nystatin surface aggregation: Relation to pore formation
    • A. Coutinho, L. Silva, A. Fedorov, and M. Prieto Cholesterol and ergosterol influence nystatin surface aggregation: relation to pore formation Biophys. J. 87 2004 3264 3276
    • (2004) Biophys. J. , vol.87 , pp. 3264-3276
    • Coutinho, A.1    Silva, L.2    Fedorov, A.3    Prieto, M.4
  • 31
    • 33646785059 scopus 로고    scopus 로고
    • Nystatin-induced lipid vesicle permeabilization is strongly dependent on sterol structure
    • L. Silva, A. Coutinho, A. Fedorov, and M. Prieto Nystatin-induced lipid vesicle permeabilization is strongly dependent on sterol structure Biochim. Biophys. Acta 1758 2006 452 459
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 452-459
    • Silva, L.1    Coutinho, A.2    Fedorov, A.3    Prieto, M.4
  • 32
    • 0342493327 scopus 로고    scopus 로고
    • Effects of vitrified and nonvitrified sugars on phosphatidylcholine fluid-to-gel phase transitions
    • K.L. Koster, Y.P. Lei, M. Anderson, S. Martin, and G. Bryant Effects of vitrified and nonvitrified sugars on phosphatidylcholine fluid-to-gel phase transitions Biophys. J. 78 2000 1932 1946
    • (2000) Biophys. J. , vol.78 , pp. 1932-1946
    • Koster, K.L.1    Lei, Y.P.2    Anderson, M.3    Martin, S.4    Bryant, G.5
  • 33
  • 34
    • 33745755109 scopus 로고
    • Phase contrast, a new method for the microscopic observation of transparent objects
    • (first part), 975-986 (second part)
    • F. Zernike Phase contrast, a new method for the microscopic observation of transparent objects Physica 9 1942 686 698 (first part), 975-986 (second part)
    • (1942) Physica , vol.9 , pp. 686-698
    • Zernike, F.1
  • 35
    • 0035997034 scopus 로고    scopus 로고
    • Mechanisms of equinatoxin II-induced transport through the membrane of a giant phospholipid vesicle
    • M. Mally, J. Majhenc, S. Svetina, and B. Žekš Mechanisms of equinatoxin II-induced transport through the membrane of a giant phospholipid vesicle Biophys. J. 83 2002 944 953
    • (2002) Biophys. J. , vol.83 , pp. 944-953
    • Mally, M.1    Majhenc, J.2    Svetina, S.3    Žekš, B.4
  • 36
    • 0027425198 scopus 로고
    • Effects of alcohol-induced lipid interdigitation on proton permeability in l-α-dipalmitoylphosphatidylcholine vesicles
    • J. Zeng, K.E. Smith, and L.G. Chong Effects of alcohol-induced lipid interdigitation on proton permeability in l-α- dipalmitoylphosphatidylcholine vesicles Biophys. J. 65 1993 1404 1414
    • (1993) Biophys. J. , vol.65 , pp. 1404-1414
    • Zeng, J.1    Smith, K.E.2    Chong, L.G.3
  • 37
    • 0025968124 scopus 로고
    • The conformation of membranes
    • R. Lipowsky The conformation of membranes Nature 349 1991 475 481
    • (1991) Nature , vol.349 , pp. 475-481
    • Lipowsky, R.1
  • 38
    • 70350769311 scopus 로고    scopus 로고
    • Vesicle budding and the origin of cellular life
    • S. Svetina Vesicle budding and the origin of cellular life Chem. Phys. Chem. 10 2009 2769 2776
    • (2009) Chem. Phys. Chem. , vol.10 , pp. 2769-2776
    • Svetina, S.1
  • 39
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • F.Y. Chen, M.T. Lee, and H.W. Huang Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 84 2003 3751 3758
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 40
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • H.W. Huang, F.Y. Chen, and M.T. Lee Molecular mechanism of peptide-induced pores in membranes Phys. Rev. Lett. 92 2004 198304
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 41
    • 18844409111 scopus 로고    scopus 로고
    • Perturbation of lipid membrane by amphipatic peptides and its role in pore formation
    • A. Zemel, A. Ben-Shaul, and S. May Perturbation of lipid membrane by amphipatic peptides and its role in pore formation Eur. Biophys. J. 34 2005 230 242
    • (2005) Eur. Biophys. J. , vol.34 , pp. 230-242
    • Zemel, A.1    Ben-Shaul, A.2    May, S.3
  • 43
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • K. Matsuzaki, O. Murase, N. Fujii, and K. Miyajima An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation Biochemistry 35 1996 11361 11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 44
    • 0021592259 scopus 로고
    • Single-length and double-length channels formed by nystatin in lipid bilayer membranes
    • M.E. Kleinberg, and A. Finkelstein Single-length and double-length channels formed by nystatin in lipid bilayer membranes J. Membr. Biol. 80 1984 257 269
    • (1984) J. Membr. Biol. , vol.80 , pp. 257-269
    • Kleinberg, M.E.1    Finkelstein, A.2
  • 45
    • 0000815976 scopus 로고
    • Determination of the effective hydrodynamic radii of small molecules by viscometry
    • S.G. Schultz, and A.K. Solomon Determination of the effective hydrodynamic radii of small molecules by viscometry J. Gen. Physiol. 44 1961 1189 1199
    • (1961) J. Gen. Physiol. , vol.44 , pp. 1189-1199
    • Schultz, S.G.1    Solomon, A.K.2
  • 46
    • 34047270717 scopus 로고    scopus 로고
    • The response of giant phospholipid vesicles to pore-forming peptide melittin
    • M. Mally, J. Majhenc, S. Svetina, and B. Žekš The response of giant phospholipid vesicles to pore-forming peptide melittin Biochim. Biophys. Acta 1768 2007 1179 1189
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1179-1189
    • Mally, M.1    Majhenc, J.2    Svetina, S.3    Žekš, B.4
  • 47
    • 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
  • 48
    • 0141865601 scopus 로고    scopus 로고
    • Dynamic tension spectroscopy and strength of biomembranes
    • E. Evans, V. Heinrich, F. Ludwig, and W. Rawicz Dynamic tension spectroscopy and strength of biomembranes Biophys. J. 85 2003 2342 2350
    • (2003) Biophys. J. , vol.85 , pp. 2342-2350
    • Evans, E.1    Heinrich, V.2    Ludwig, F.3    Rawicz, W.4
  • 49
    • 0025969267 scopus 로고
    • Potassium-selective amphotericin B channels are predominant in vesicles regardless of sidedness
    • S.C. Hartsel, S.K. Benz, S.K. Peterson, and B.S. Whyte Potassium-selective amphotericin B channels are predominant in vesicles regardless of sidedness Biochemistry 30 1991 77 82
    • (1991) Biochemistry , vol.30 , pp. 77-82
    • Hartsel, S.C.1    Benz, S.K.2    Peterson, S.K.3    Whyte, B.S.4
  • 50
    • 0031712650 scopus 로고    scopus 로고
    • Lipid and stress dependence of amphotericin B ion selective channels in sterol-free membranes
    • T. Ruckwardt, J. Scott, P. Scott, P. Mikulecky, and S.C. Hartsel Lipid and stress dependence of amphotericin B ion selective channels in sterol-free membranes Biochim. Biophys. Acta 1372 1998 283 288
    • (1998) Biochim. Biophys. Acta , vol.1372 , pp. 283-288
    • Ruckwardt, T.1    Scott, J.2    Scott, P.3    Mikulecky, P.4    Hartsel, S.C.5
  • 52
    • 0000693135 scopus 로고
    • Induction of an interdigitated gel phase in fully hydrated phosphatidylcholine bilayers
    • T.J. McIntosh, R.V. McDaniel, and S.A. Simon Induction of an interdigitated gel phase in fully hydrated phosphatidylcholine bilayers Biochim. Biophys. Acta 731 1983 109 114
    • (1983) Biochim. Biophys. Acta , vol.731 , pp. 109-114
    • McIntosh, T.J.1    McDaniel, R.V.2    Simon, S.A.3
  • 53
    • 0021761592 scopus 로고
    • Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions
    • S.A. Simon, and T.J. McIntosh Interdigitated hydrocarbon chain packing causes the biphasic transition behavior in lipid/alcohol suspensions Biochim. Biophys. Acta 773 1984 169 172
    • (1984) Biochim. Biophys. Acta , vol.773 , pp. 169-172
    • Simon, S.A.1    McIntosh, T.J.2


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