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Volumn 367, Issue 1, 2007, Pages 49-55

Exploring the effect of cholesterol in lipid bilayer membrane on the melittin penetration mechanism

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHOLESTEROL; PEPTIDES; PHOSPHOLIPIDS;

EID: 34250613536     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.04.039     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 33845456716 scopus 로고    scopus 로고
    • Modeling leakage kinetics from multilamellar vesicles for membrane permeability determination: Application to glucose
    • Faure C., Nallet F., Roux D., Milner S.T., Gauffre F., Olea D., and Lambert O. Modeling leakage kinetics from multilamellar vesicles for membrane permeability determination: Application to glucose. Biophys. J. 91 (2006) 4340-4349
    • (2006) Biophys. J. , vol.91 , pp. 4340-4349
    • Faure, C.1    Nallet, F.2    Roux, D.3    Milner, S.T.4    Gauffre, F.5    Olea, D.6    Lambert, O.7
  • 2
    • 33845571063 scopus 로고    scopus 로고
    • Modeling the structure of the StART domains of MLN64 and StAR proteins in complex with cholesterol
    • Murcia M., Faraldo-Gomez J.D., Maxfield F.R., and Roux B. Modeling the structure of the StART domains of MLN64 and StAR proteins in complex with cholesterol. J. Lipid Res. 47 (2006) 2614-2630
    • (2006) J. Lipid Res. , vol.47 , pp. 2614-2630
    • Murcia, M.1    Faraldo-Gomez, J.D.2    Maxfield, F.R.3    Roux, B.4
  • 4
    • 0345575646 scopus 로고    scopus 로고
    • Adhesion kinetics of functionalized vesicles and mammalian cells: a comparative study
    • Reiss B., Janshoff A., Steinem C., Seebach J., and Wegener J. Adhesion kinetics of functionalized vesicles and mammalian cells: a comparative study. Langmuir 19 (2003) 1816-1823
    • (2003) Langmuir , vol.19 , pp. 1816-1823
    • Reiss, B.1    Janshoff, A.2    Steinem, C.3    Seebach, J.4    Wegener, J.5
  • 5
    • 0034299213 scopus 로고    scopus 로고
    • Method for Fabricating Supported Bilayer Lipid Membranes on Gold
    • Lahiri J., Kalal P., Frutos A.G., Jonas S.J., and Schaeffler R. Method for Fabricating Supported Bilayer Lipid Membranes on Gold. Langmuir 16 (2000) 7805-7810
    • (2000) Langmuir , vol.16 , pp. 7805-7810
    • Lahiri, J.1    Kalal, P.2    Frutos, A.G.3    Jonas, S.J.4    Schaeffler, R.5
  • 6
    • 4344667966 scopus 로고    scopus 로고
    • Fluid Biomembranes Supported on Nanoporous Aerogel/Xerogel Substrates
    • Weng K.C., Stalgren J.J.R., Duval D.J., Risbud S.H., and Frank C.W. Fluid Biomembranes Supported on Nanoporous Aerogel/Xerogel Substrates. Langmuir 20 (2004) 7232-7239
    • (2004) Langmuir , vol.20 , pp. 7232-7239
    • Weng, K.C.1    Stalgren, J.J.R.2    Duval, D.J.3    Risbud, S.H.4    Frank, C.W.5
  • 8
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon J.M., Kolodziejek J., and Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim. Biophys. Acta 1696 (2004) 1-14
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 9
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee M.T., Chen F.Y., and Huang H.W. Energetics of pore formation induced by membrane active peptides. Biochemistry 43 (2004) 3590-3599
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.T.1    Chen, F.Y.2    Huang, H.W.3
  • 11
    • 22444437008 scopus 로고    scopus 로고
    • Vesicular polydiacetylene sensor for colorimetric signaling of bacterial pore-forming toxin
    • Ma G.Y., and Cheng Q. Vesicular polydiacetylene sensor for colorimetric signaling of bacterial pore-forming toxin. Langmuir 21 (2005) 6123-6126
    • (2005) Langmuir , vol.21 , pp. 6123-6126
    • Ma, G.Y.1    Cheng, Q.2
  • 12
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • Hristova K., Dempsey C.E., and White S.H. Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys. J. 80 (2001) 801-811
    • (2001) Biophys. J. , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 13
    • 0242290843 scopus 로고    scopus 로고
    • Pathways of lipid vesicle deposition on solid surface: a combined QCM-D and AFM study
    • Richter R., Mukhopadhyay A., and Brisson A. Pathways of lipid vesicle deposition on solid surface: a combined QCM-D and AFM study. Biophys. J. 85 (2003) 3035-3047
    • (2003) Biophys. J. , vol.85 , pp. 3035-3047
    • Richter, R.1    Mukhopadhyay, A.2    Brisson, A.3
  • 14
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White S.H., and Wimley W.C. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta 1376 (1998) 339-352
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 15
    • 16344384943 scopus 로고    scopus 로고
    • Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR
    • Toraya S., Nishimura K., and Naito A. Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR. Biophys. J. 87 (2004) 3323-3335
    • (2004) Biophys. J. , vol.87 , pp. 3323-3335
    • Toraya, S.1    Nishimura, K.2    Naito, A.3
  • 16
    • 0029042292 scopus 로고
    • Study of vesicle leakage induced by melittin
    • Benachir T., and Lafleur M. Study of vesicle leakage induced by melittin. Biochim. Biophys. Acta 1235 (1995) 452-460
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 452-460
    • Benachir, T.1    Lafleur, M.2
  • 17
    • 0037417761 scopus 로고    scopus 로고
    • Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis
    • Allende D., and McIntosh T.J. Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis. Biochemistry 42 (2003) 1101-1108
    • (2003) Biochemistry , vol.42 , pp. 1101-1108
    • Allende, D.1    McIntosh, T.J.2
  • 18
    • 0029947537 scopus 로고    scopus 로고
    • Influence of lipid chain unsaturation on melittin-induced micellization
    • Monette M., and Lafleur M. Influence of lipid chain unsaturation on melittin-induced micellization. Biophys. J. 70 (1996) 2195-2202
    • (1996) Biophys. J. , vol.70 , pp. 2195-2202
    • Monette, M.1    Lafleur, M.2
  • 20
    • 0034694971 scopus 로고    scopus 로고
    • Supported planar bilayer formation by vesicle fusion: the interaction of phospholipid vesicles with surfaces and the effect of gramicidin on bilayer properties using atomoc force microscopy
    • Leonenko Z.V., Carnini A., and Cramb D.T. Supported planar bilayer formation by vesicle fusion: the interaction of phospholipid vesicles with surfaces and the effect of gramicidin on bilayer properties using atomoc force microscopy. Biochim. Biophys. Acta 1509 (2000) 131-147
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 131-147
    • Leonenko, Z.V.1    Carnini, A.2    Cramb, D.T.3
  • 21
    • 27744511675 scopus 로고    scopus 로고
    • Morphological Behavior of Lipid Bilayers Induced by Melittin near the Phase Transition Temperature
    • Toraya S., Nagao T., Norisada K., Tuzi S., Saito H., Izumi S., and Naito A. Morphological Behavior of Lipid Bilayers Induced by Melittin near the Phase Transition Temperature. Biophys. J. 89 (2005) 3214-3222
    • (2005) Biophys. J. , vol.89 , pp. 3214-3222
    • Toraya, S.1    Nagao, T.2    Norisada, K.3    Tuzi, S.4    Saito, H.5    Izumi, S.6    Naito, A.7
  • 22
    • 0034866616 scopus 로고    scopus 로고
    • The energetics of binding of a signal peptide to lipid bilayers: the role of bilayer properties
    • McIntosh T.J., Vidal A., and Simon S.A. The energetics of binding of a signal peptide to lipid bilayers: the role of bilayer properties. Biochem. Soc. Trans. 29 (2001) 594-598
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 594-598
    • McIntosh, T.J.1    Vidal, A.2    Simon, S.A.3
  • 23
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1031 (1990) 143-161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 24
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 25
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides
    • Papo N., and Shai Y. Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 42 (2003) 458-466
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 26
    • 16344382233 scopus 로고    scopus 로고
    • Cholesterol and ergosterol influence nystatin surface aggregation: relation to pore formation
    • Coutinho A., Silva L., Fedorov A., and Prieto M. 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
  • 28
    • 0034763782 scopus 로고    scopus 로고
    • Solid-state NMR structure determination of melittin in a lipid environment
    • Lam Y.H., Wassall S.R., Morton C.J., Smith R., and Separovic F. Solid-state NMR structure determination of melittin in a lipid environment. Biophys. J. 81 (2001) 2752-2761
    • (2001) Biophys. J. , vol.81 , pp. 2752-2761
    • Lam, Y.H.1    Wassall, S.R.2    Morton, C.J.3    Smith, R.4    Separovic, F.5
  • 29
    • 33750171887 scopus 로고    scopus 로고
    • Effect of ionic strength on the organization and dynamics of membrane-bound melittin
    • Raghuraman H., Ganguly S., and Chattopadhyay A. Effect of ionic strength on the organization and dynamics of membrane-bound melittin. Biophys. Chem. 124 (2006) 115-124
    • (2006) Biophys. Chem. , vol.124 , pp. 115-124
    • Raghuraman, H.1    Ganguly, S.2    Chattopadhyay, A.3
  • 31
    • 33746803326 scopus 로고    scopus 로고
    • Cholesterol-Phospholipid Association in Fluid Bilayers: A Thermodynamic Analysis from Nearest-Neighbor Recognition Measurements
    • Zhang J., Cao H., Jing B., Almeida P.F., and Regen S.L. Cholesterol-Phospholipid Association in Fluid Bilayers: A Thermodynamic Analysis from Nearest-Neighbor Recognition Measurements. Biophys. J. 91 (2006) 1402-1406
    • (2006) Biophys. J. , vol.91 , pp. 1402-1406
    • Zhang, J.1    Cao, H.2    Jing, B.3    Almeida, P.F.4    Regen, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.