메뉴 건너뛰기




Volumn 1778, Issue 6, 2008, Pages 1460-1466

Cholesterol, lanosterol, and ergosterol attenuate the membrane association of LL-37(W27F) and temporin L

Author keywords

Antimicrobial peptides; Fluorescence spectroscopy; Liposomes, Hydrophobicity; Sterols

Indexed keywords

ADENOSINE PHOSPHATE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CHOLESTEROL; ERGOSTEROL; LANOSTEROL; POLYPEPTIDE ANTIBIOTIC AGENT; TEMPORIN L;

EID: 43649090328     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.02.014     Document Type: Article
Times cited : (50)

References (47)
  • 1
    • 2442494292 scopus 로고    scopus 로고
    • Influence of cholesterol and ergosterol on membrane dynamics: a fluorescence approach
    • Arora A., Raghuraman H., and Chattopadhyay A. Influence of cholesterol and ergosterol on membrane dynamics: a fluorescence approach. Biochim. Biophys. Acta 318 (2004) 920-926
    • (2004) Biochim. Biophys. Acta , vol.318 , pp. 920-926
    • Arora, A.1    Raghuraman, H.2    Chattopadhyay, A.3
  • 2
  • 3
    • 0141939627 scopus 로고    scopus 로고
    • Differential properties of the sterols cholesterol, ergosterol, sitosterol, trans-7-dehydrocholesterol and lanosterol on DPPC bilayer order
    • Bernsdorff C., and Winter R. Differential properties of the sterols cholesterol, ergosterol, sitosterol, trans-7-dehydrocholesterol and lanosterol on DPPC bilayer order. J. Phys. Chem., B. 107 (2003) 10658
    • (2003) J. Phys. Chem., B. , vol.107 , pp. 10658
    • Bernsdorff, C.1    Winter, R.2
  • 5
    • 0141897969 scopus 로고
    • Florkin M., and Stoltz E.H. (Eds), Elsevier, New York
    • Kritchevsky D. In: Florkin M., and Stoltz E.H. (Eds). Comprehensive Biochemistry Vol. 10 (1963), Elsevier, New York 1-22
    • (1963) Comprehensive Biochemistry , vol.10 , pp. 1-22
    • Kritchevsky, D.1
  • 7
    • 0018946930 scopus 로고
    • Effect of alkyl-substituted precursors of cholesterol on artificial and natural membranes and on the viability of mycoplasma capricolum
    • Dahl C.E., Dahl J.S., and Bloch K. Effect of alkyl-substituted precursors of cholesterol on artificial and natural membranes and on the viability of mycoplasma capricolum. Biochemistry 19 (1980) 1462-1467
    • (1980) Biochemistry , vol.19 , pp. 1462-1467
    • Dahl, C.E.1    Dahl, J.S.2    Bloch, K.3
  • 8
    • 0342576225 scopus 로고    scopus 로고
    • The effect of side chain analogues of cholesterol on the thermotropic phase behavior of SOPC bilayers. A differential scanning calorimetric study
    • Vilcheze C., Mcmullen T.P.W., McElhaney R.N., and Bittman R. The effect of side chain analogues of cholesterol on the thermotropic phase behavior of SOPC bilayers. A differential scanning calorimetric study. Biochim. Biophys. Acta 1279 (1996) 235-242
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 235-242
    • Vilcheze, C.1    Mcmullen, T.P.W.2    McElhaney, R.N.3    Bittman, R.4
  • 9
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective.
    • Bloom M., Evans E., and Mouritsen O.G. Physical properties of the fluid lipid-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
  • 11
    • 0037117885 scopus 로고    scopus 로고
    • The effect of cholesterol, lanosterol, and ergosterol on lecithin bilayer mechanical properties at molecular and microscopic dimensions: a solid-state NMR and micropipet study
    • Endress E., Bayer S., Prechtel K., Maier C., Merkel R., and Bayerl T.M. The effect of cholesterol, lanosterol, and ergosterol on lecithin bilayer mechanical properties at molecular and microscopic dimensions: a solid-state NMR and micropipet study. Langmuir 18 (2002) 3293-3299
    • (2002) Langmuir , vol.18 , pp. 3293-3299
    • Endress, E.1    Bayer, S.2    Prechtel, K.3    Maier, C.4    Merkel, R.5    Bayerl, T.M.6
  • 12
    • 11244267130 scopus 로고    scopus 로고
    • Vesicle fluctuation analysis of the effects of sterols on membrane bending rigidity
    • Henriksen J., Rowat A.C., and Ipsen J.H. Vesicle fluctuation analysis of the effects of sterols on membrane bending rigidity. Eur. Biophys. J. 33 (2004) 732-741
    • (2004) Eur. Biophys. J. , vol.33 , pp. 732-741
    • Henriksen, J.1    Rowat, A.C.2    Ipsen, J.H.3
  • 13
    • 33751210938 scopus 로고    scopus 로고
    • Comparative calorimetric and spectroscopic studies of the effects of lanosterol and cholesterol on the thermotropic phase behavior and organization of dipalmitoylphosphatidylcholine bilayer membranes
    • Mannock D.A., Lewis R.N.A.H., and McElhaney R.N. Comparative calorimetric and spectroscopic studies of the effects of lanosterol and cholesterol on the thermotropic phase behavior and organization of dipalmitoylphosphatidylcholine bilayer membranes. Biophys. J. 91 (2006) 3327-3340
    • (2006) Biophys. J. , vol.91 , pp. 3327-3340
    • Mannock, D.A.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 14
    • 33847691929 scopus 로고    scopus 로고
    • Differential effects of cholesterol, ergosterol and lanosterol on a dipalmitoylphosphatidylcholine membrane: a molecular dynamics simulation study
    • Cournia Z., Ullmann G.M., and Smith J.C. Differential effects of cholesterol, ergosterol and lanosterol on a dipalmitoylphosphatidylcholine membrane: a molecular dynamics simulation study. J. Phys. Chem., B. 111 (2007) 1786-1801
    • (2007) J. Phys. Chem., B. , vol.111 , pp. 1786-1801
    • Cournia, Z.1    Ullmann, G.M.2    Smith, J.C.3
  • 15
    • 21144453569 scopus 로고    scopus 로고
    • The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study
    • Hsueh Y.W., Gilbert K., Trandum C., Zuckermann M., and Thewalt J. The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study. Biophys. J. 88 (2005) 1799-1808
    • (2005) Biophys. J. , vol.88 , pp. 1799-1808
    • Hsueh, Y.W.1    Gilbert, K.2    Trandum, C.3    Zuckermann, M.4    Thewalt, J.5
  • 16
    • 33646177411 scopus 로고    scopus 로고
    • o) phase of phosphatidylcholine/cholesterol membranes: a variable temperature multinuclear solid-state NMR and X-Ray diffraction study
    • o) phase of phosphatidylcholine/cholesterol membranes: a variable temperature multinuclear solid-state NMR and X-Ray diffraction study. Biophys. J. 90 (2006) 2383-2393
    • (2006) Biophys. J. , vol.90 , pp. 2383-2393
    • Clarke, J.A.1    Heron, A.J.2    Seddon, J.M.3    Law, R.V.4
  • 17
    • 0034620610 scopus 로고    scopus 로고
    • The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
    • Xu X., and London E. The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation. Biochemistry 39 (2000) 843-849
    • (2000) Biochemistry , vol.39 , pp. 843-849
    • Xu, X.1    London, E.2
  • 19
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle P.L. Cholesterol and the cell membrane. Biochim. Biophys. Acta 822 (1985) 267-287
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 21
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E.W., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16 (1998) 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 22
    • 33847668734 scopus 로고    scopus 로고
    • Fluorescent temporin B derivative and its binding to liposomes
    • Sood R., Domanov Y., and Kinnunen P.K.J. Fluorescent temporin B derivative and its binding to liposomes. J. Fluorescence 17 (2007) 223-234
    • (2007) J. Fluorescence , vol.17 , pp. 223-234
    • Sood, R.1    Domanov, Y.2    Kinnunen, P.K.J.3
  • 23
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 24
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity
    • Sitaram N., and Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim. Biophys. Acta 1462 (1999) 29-54
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 25
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non cell selective activity
    • Oren Z., Lerman J.C., Gudmundsson G.H., Agerberth B., and Shai Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non cell selective activity. Biochem. J. 341 (1999) 501-513
    • (1999) Biochem. J. , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 26
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Durr U.H., Sudheendra U.S., and Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta. 1758 (2006) 1408-1425
    • (2006) Biochim. Biophys. Acta. , vol.1758 , pp. 1408-1425
    • Durr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 27
    • 3042743487 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability, and viability of Escherichia coli
    • Mangoni M.L., Papo N., Barra D., Simmaco M., Bozz A., Giulio A.D., and Rinaldi A.C. Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability, and viability of Escherichia coli. Biochem. J. 380 (2004) 859-865
    • (2004) Biochem. J. , vol.380 , pp. 859-865
    • Mangoni, M.L.1    Papo, N.2    Barra, D.3    Simmaco, M.4    Bozz, A.5    Giulio, A.D.6    Rinaldi, A.C.7
  • 29
    • 0037067706 scopus 로고    scopus 로고
    • Binding of antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • Zhao H., and Kinnunen P.K.J. Binding of antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 277 (2002) 25170-25177
    • (2002) J. Biol. Chem. , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.J.2
  • 30
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action
    • Zhao H., Sood R., Jutila A., Bose S., Fimland G., Meyer J.N., and Kinnunen P.K.J. Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action. Biochim. Biophys. Acta 1758 (2006) 1461-1474
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5    Meyer, J.N.6    Kinnunen, P.K.J.7
  • 31
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide magainin 2
    • Matsuzaki K., Sugishita K.I., Fujii N., and Miyajima K. Molecular basis for membrane selectivity of an antimicrobial peptide magainin 2. Biochemistry 34 (1995) 3423-3429
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.I.2    Fujii, N.3    Miyajima, K.4
  • 32
    • 0037007001 scopus 로고    scopus 로고
    • Interactions of the antimicrobial peptides temporins with model biomembranes. Comparison of temporins B and L
    • Zhao H., Rinaldi A.C., Giulio A.D., Simmaco M., and Kinnunen P.K.J. Interactions of the antimicrobial peptides temporins with model biomembranes. Comparison of temporins B and L. Biochemistry 41 (2002) 4425-4436
    • (2002) Biochemistry , vol.41 , pp. 4425-4436
    • Zhao, H.1    Rinaldi, A.C.2    Giulio, A.D.3    Simmaco, M.4    Kinnunen, P.K.J.5
  • 33
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J., Gudmundson G.H., Rottenberg M.E., Berndt K.D., and Agerberth B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273 (1998) 3718-3724
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 34
    • 14344250143 scopus 로고    scopus 로고
    • Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid like fibers
    • Zhao H., Jutila A., Nurminen T., Wickstrom S.A., Keski-Oja J., and Kinnunen P.K.J. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid like fibers. Biochemistry 44 (2005) 2857-2863
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5    Kinnunen, P.K.J.6
  • 35
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H., Tuominen E.K.J., and Kinnunen P.K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 36
    • 0020648725 scopus 로고
    • Sterol structure and membrane function
    • Bloch K. Sterol structure and membrane function. CRC Crit. Rev. Biochem. 14 (1983) 47-92
    • (1983) CRC Crit. Rev. Biochem. , vol.14 , pp. 47-92
    • Bloch, K.1
  • 38
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide LL-37
    • Wildman K.A.H., Lee D.K., and Ramamoorthy A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide LL-37. Biochemistry 42 (2003) 6545-6558
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Wildman, K.A.H.1    Lee, D.K.2    Ramamoorthy, A.3
  • 39
    • 37349002470 scopus 로고    scopus 로고
    • Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization
    • Mason A.J., Marquette A., and Bechinger B. Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization. Biophys. J. 93 (2007) 4289-4299
    • (2007) Biophys. J. , vol.93 , pp. 4289-4299
    • Mason, A.J.1    Marquette, A.2    Bechinger, B.3
  • 41
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • Karoon A.I.P.M.D., Soekarjo M.W., Gier J.D., and Kruijff B.D. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 29 (1990) 8229-8240
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • Karoon, A.I.P.M.D.1    Soekarjo, M.W.2    Gier, J.D.3    Kruijff, B.D.4
  • 42
    • 33847798446 scopus 로고
    • Fluorescence quenching of indole and model micelle systems
    • Eftink M.R., and Ghiron C.A. Fluorescence quenching of indole and model micelle systems. J. Phys. Chem. 80 (1976) 486-493
    • (1976) J. Phys. Chem. , vol.80 , pp. 486-493
    • Eftink, M.R.1    Ghiron, C.A.2
  • 44
    • 0035073937 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol
    • Smondyrev A.M., and Berkowitz M.L. Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol. Biophys. J. 80 (2001) 1649-1658
    • (2001) Biophys. J. , vol.80 , pp. 1649-1658
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 45
    • 0015505766 scopus 로고
    • Monolayer interactions of individual lecithins with natural sterols
    • Ghosh D., and Tinoco J. Monolayer interactions of individual lecithins with natural sterols. Biochim. Biophys. Acta 266 (1972) 41-49
    • (1972) Biochim. Biophys. Acta , vol.266 , pp. 41-49
    • Ghosh, D.1    Tinoco, J.2
  • 46
    • 0015513392 scopus 로고
    • The effect of sterol structure on the permeability of liposomes to glucose, glycerol and Rb+
    • Demel R.A., Bruckdorfer K.R., and Van Deenen L.L.M. The effect of sterol structure on the permeability of liposomes to glucose, glycerol and Rb+. Biochim. Biophys. Acta 255 (1972) 321-330
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 321-330
    • Demel, R.A.1    Bruckdorfer, K.R.2    Van Deenen, L.L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.