메뉴 건너뛰기




Volumn 185, Issue , 2015, Pages 99-108

Melittin modifies bending elasticity in an unexpected way

Author keywords

Bending elasticity; Diacylglycerophosphatidylcholine; Giant vesicles; Lysis; Melittin; X ray diffraction

Indexed keywords

ALAMETHICIN; MELITTIN; POLYPEPTIDE ANTIBIOTIC AGENT; 1-STEAROYL-2-OLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE; LIPID BILAYER; LIPOSOME; PHOSPHATIDYLCHOLINE;

EID: 84921485816     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2014.05.004     Document Type: Article
Times cited : (16)

References (80)
  • 1
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • Allende, D., Simon, S.A., McIntosh, T.J., 2005. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys. J. 88, 1828-1837.
    • (2005) Biophys. J. , vol.88 , pp. 1828-1837
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 2
    • 0037274943 scopus 로고    scopus 로고
    • Bilayer interfacial properties modulate the binding of amphipathic peptides
    • Allende, D., Vidal, A., Simon, S.A., McIntosh, T.J., 2003. Bilayer interfacial properties modulate the binding of amphipathic peptides. Chem. Phys. Lipids 122, 65-76.
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 65-76
    • Allende, D.1    Vidal, A.2    Simon, S.A.3    McIntosh, T.J.4
  • 3
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B., 1997. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156, 197-211.
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 4
    • 68749115077 scopus 로고    scopus 로고
    • Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape
    • Bechinger, B., 2009. Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape. Curr. Opin. Colloid Interface Sci. 14, 349-355.
    • (2009) Curr. Opin. Colloid Interface Sci. , vol.14 , pp. 349-355
    • Bechinger, B.1
  • 5
    • 79953805263 scopus 로고    scopus 로고
    • Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations
    • Bechinger, B., 2011. Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations. J. Pept. Sci. 17, 306-314.
    • (2011) J. Pept. Sci. , vol.17 , pp. 306-314
    • Bechinger, B.1
  • 6
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B., Lohner, K., 2006. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta (BBA): Biomembr. 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 7
    • 0015242989 scopus 로고
    • Structure of the nerve myelin membrane: Proof of the low resolution profile
    • Blaurock, A.E., 1971. Structure of the nerve myelin membrane: proof of the low resolution profile. J. Mol. Biol. 56, 35-52.
    • (1971) J. Mol. Biol. , vol.56 , pp. 35-52
    • Blaurock, A.E.1
  • 10
    • 0032942642 scopus 로고    scopus 로고
    • The amphipathic helix concept: Length effects on ideally amphipathic LiKj(i = 2j) peptides to acquire optimal hemolytic activity
    • Castano, S., Cornut, I., Büttner, K., Dasseux, J.L., Dufourcq, J., 1999. The amphipathic helix concept: length effects on ideally amphipathic LiKj(i = 2j) peptides to acquire optimal hemolytic activity. Biochim. Biophys. Acta (BBA): Biomembr. 1416, 161-175.
    • (1999) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1416 , pp. 161-175
    • Castano, S.1    Cornut, I.2    Büttner, K.3    Dasseux, J.L.4    Dufourcq, J.5
  • 11
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F.-Y., Lee, M.-T., Huang, H.W., 2002. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82, 908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 12
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F.-Y., Lee, M.-T., Huang, H.W., 2003. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84, 3751-3758.
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 13
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe, M., Wieprecht, T., 1999. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta (BBA): Biomembr. 1462, 71-87.
    • (1999) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 14
    • 0019497821 scopus 로고
    • Design, synthesis, and characterization of a cytotoxic peptide with melittin-like activity
    • DeGrado, W.F., Kezdy, F.J., Kaiser, E.T., 1981. Design, synthesis, and characterization of a cytotoxic peptide with melittin-like activity. J. Am. Chem. Soc. 103, 679-681.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 679-681
    • DeGrado, W.F.1    Kezdy, F.J.2    Kaiser, E.T.3
  • 15
    • 0025217893 scopus 로고
    • The action of melittin on membranes
    • Dempsey, C.E., 1990. The action of melittin on membranes. Biochim. Biophys. Acta 1031, 143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 16
    • 0022516431 scopus 로고
    • Morphological changes of phosphatidylcholine bilayers induced by melittin: Vesicularization, fusion, discoidal particles
    • Dufourcq, J., Faucon, J.F., Fourche, G., Dasseux, J.L., Le Maire, M., Gulik-Krzywicki, T., 1986. Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles. Biochim. Biophys. Acta 859, 33-48.
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 33-48
    • Dufourcq, J.1    Faucon, J.F.2    Fourche, G.3    Dasseux, J.L.4    Le Maire, M.5    Gulik-Krzywicki, T.6
  • 17
    • 67349142581 scopus 로고    scopus 로고
    • Membrane permeabilization by Islet Amyloid Polypeptide
    • Engel, M.F.M., 2009. Membrane permeabilization by Islet Amyloid Polypeptide. Chem. Phys. Lipids 160, 1-10.
    • (2009) Chem. Phys. Lipids , vol.160 , pp. 1-10
    • Engel, M.F.M.1
  • 18
    • 0018487558 scopus 로고
    • The self-association of melittin and its binding to lipids: An intrinsic fluorescence polarization study
    • Faucon, J.F., Dufourcq, J., Lussan, C., 1979. The self-association of melittin and its binding to lipids: an intrinsic fluorescence polarization study. FEBS Lett. 102, 187-190.
    • (1979) FEBS Lett. , vol.102 , pp. 187-190
    • Faucon, J.F.1    Dufourcq, J.2    Lussan, C.3
  • 19
    • 84957313755 scopus 로고
    • Temperature and chain length effects on bending elasticity of phosphatidylcholine bilayers
    • Fernandez-Puente, L., Bivas, I., Mitov, M.D., Méléard, P., 1994. Temperature and chain length effects on bending elasticity of phosphatidylcholine bilayers. Europhys. Lett. 28, 181.
    • (1994) Europhys. Lett. , vol.28 , pp. 181
    • Fernandez-Puente, L.1    Bivas, I.2    Mitov, M.D.3    Méléard, P.4
  • 20
    • 0018597218 scopus 로고
    • The structure of lipid bilayers and the effects of general anesthetics: An X-ray and neutron diffraction study
    • Franks, N.P., Lieb, W.R., 1979. The structure of lipid bilayers and the effects of general anesthetics: an X-ray and neutron diffraction study. J. Mol. Biol. 133, 469-500.
    • (1979) J. Mol. Biol. , vol.133 , pp. 469-500
    • Franks, N.P.1    Lieb, W.R.2
  • 21
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann, E., 1972. Bee and wasp venoms. Science 177, 314-322.
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 22
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He, K., Ludtke, S.J., Worcester, D.L., Huang, H.W., 1996. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70, 2659-2666.
    • (1996) Biophys. J. , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 23
    • 5244231192 scopus 로고
    • The size of bilayer vesicles generated by sonication
    • Helfrich, W., 1974. The size of bilayer vesicles generated by sonication. Phys. Lett. A 50, 115-116.
    • (1974) Phys. Lett. , vol.50 , pp. 115-116
    • Helfrich, W.1
  • 24
    • 0031006189 scopus 로고    scopus 로고
    • Effect of changing the size of lipid headgroup on peptide insertion into membranes
    • Heller, W.T., He, K., Ludtke, S.J., Harroun, T.A., Huang, H.W., 1997. Effect of changing the size of lipid headgroup on peptide insertion into membranes. Biophys. J. 73, 239-244.
    • (1997) Biophys. J. , vol.73 , pp. 239-244
    • Heller, W.T.1    He, K.2    Ludtke, S.J.3    Harroun, T.A.4    Huang, H.W.5
  • 27
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang, H.W., 2006. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta (BBA): Biomembr. 1758, 1292-1302.
    • (2006) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 28
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang, H.W., Chen, F.-Y., Lee, M.-T., 2004. Molecular mechanism of peptide-induced pores in membranes. Phys. Rev. Lett. 92, 198304.
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.-Y.2    Lee, M.-T.3
  • 29
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R.E., White, S.H., 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry 28, 3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 30
    • 0025870831 scopus 로고
    • Aggregation state of melittin in lipid vesicle membranes
    • John, E., Jähnig, F., 1991. Aggregation state of melittin in lipid vesicle membranes. Biophys. J. 60, 319-328.
    • (1991) Biophys. J. , vol.60 , pp. 319-328
    • John, E.1    Jähnig, F.2
  • 32
    • 80052268628 scopus 로고    scopus 로고
    • Fluid phase lipid areas and bilayer thicknesses of commonly used phosphatidylcholines as a function of temperature
    • Kučerka, N., Nieh, M.-P., Katsaras, J., 2011. Fluid phase lipid areas and bilayer thicknesses of commonly used phosphatidylcholines as a function of temperature. Biochim. Biophys. Acta (BBA): Biomembr. 1808, 2761-2771.
    • (2011) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1808 , pp. 2761-2771
    • Kučerka, N.1    Nieh, M.-P.2    Katsaras, J.3
  • 33
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • Kuchinka, E., Seelig, J., 1989. Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation. Biochemistry 28, 4216-4221.
    • (1989) Biochemistry , vol.28 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 34
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee, M.-T., Chen, F.-Y., Huang, H.W., 2004. Energetics of pore formation induced by membrane active peptides. Biochemistry 43, 3590-3599.
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.-T.1    Chen, F.-Y.2    Huang, H.W.3
  • 35
    • 28444488982 scopus 로고    scopus 로고
    • Many-body effect of antimicrobial peptides: On the correlation between lipid's spontaneous curvature and pore formation
    • Lee, M.-T., Hung, W.-C., Chen, F.-Y., Huang, H.W., 2005. Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formation. Biophys. J. 89, 4006-4016.
    • (2005) Biophys. J. , vol.89 , pp. 4006-4016
    • Lee, M.-T.1    Hung, W.-C.2    Chen, F.-Y.3    Huang, H.W.4
  • 36
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • Lee, M.-T., Hung, W.-C., Chen, F.-Y., Huang, H.W., 2008. Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides. Proc. Natl. Acad. Sci. U.S.A. 105, 5087-5092.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5087-5092
    • Lee, M.-T.1    Hung, W.-C.2    Chen, F.-Y.3    Huang, H.W.4
  • 37
    • 0001276053 scopus 로고
    • Curvature instability in membranes
    • Leibler, S., 1986. Curvature instability in membranes. J. Phys. 47, 507-516.
    • (1986) J. Phys. , vol.47 , pp. 507-516
    • Leibler, S.1
  • 38
  • 39
    • 33751222275 scopus 로고    scopus 로고
    • Structure of magainin and alamethicin in model membranes studied by X-ray reflectivity
    • Li, C., Salditt, T., 2006. Structure of magainin and alamethicin in model membranes studied by X-ray reflectivity. Biophys. J. 91, 3285-3300.
    • (2006) Biophys. J. , vol.91 , pp. 3285-3300
    • Li, C.1    Salditt, T.2
  • 41
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic α-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
    • Mahalka, A.K., Kinnunen, P.K.J., 2009. Binding of amphipathic α-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim. Biophys. Acta (BBA): Biomembr. 1788, 1600-1609.
    • (2009) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.J.2
  • 42
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K., 1998. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta (BBA): Biomembr. 1376, 391-400.
    • (1998) Biochim. Biophys. Acta (BBA): Biomembr. , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 43
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K., Yoneyama, S., Miyajima, K., 1997. Pore formation and translocation of melittin. Biophys. J. 73, 831-838.
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 44
    • 0023057572 scopus 로고
    • Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers
    • McIntosh, T.J., Simon, S.A., 1986. Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers. Biochemistry 25, 4948-4952.
    • (1986) Biochemistry , vol.25 , pp. 4948-4952
    • McIntosh, T.J.1    Simon, S.A.2
  • 45
    • 71549117067 scopus 로고    scopus 로고
    • Giant unilamellar vesicle electroformation: From lipid mixtures to native membranes under physiological conditions
    • Méléard, P., Bagatolli, L.A., Pott, T., Nejat, D., 2009. Giant unilamellar vesicle electroformation: from lipid mixtures to native membranes under physiological conditions. Methods Enzymol. 465, 161-176.
    • (2009) Methods Enzymol. , vol.465 , pp. 161-176
    • Méléard, P.1    Bagatolli, L.A.2    Pott, T.3    Nejat, D.4
  • 46
  • 48
    • 84957932559 scopus 로고    scopus 로고
    • Advantages of statistical analysis of giant vesicle flickering for bending elasticity measurements
    • Méléard, P., Pott, T., Bouvrais, H., Ipsen, J.H., 2011. Advantages of statistical analysis of giant vesicle flickering for bending elasticity measurements. Eur. Phys. J. E 34, 1-14.
    • (2011) Eur. Phys. J. E , vol.34 , pp. 1-14
    • Méléard, P.1    Pott, T.2    Bouvrais, H.3    Ipsen, J.H.4
  • 49
    • 84907101719 scopus 로고    scopus 로고
    • Bending rigidity of phosphatidylserine-containing lipid bilayers in acidic aqueous solutions
    • In press
    • Mitkova, D., Marukovich, N., Ermakov, Y.A., Vitkova, V., 2014. Bending rigidity of phosphatidylserine-containing lipid bilayers in acidic aqueous solutions. Colloids Surf. A, In press.
    • (2014) Colloids Surf. A
    • Mitkova, D.1    Marukovich, N.2    Ermakov, Y.A.3    Vitkova, V.4
  • 50
    • 0033151158 scopus 로고    scopus 로고
    • Absence of a vestigial vapor pressure paradox
    • Nagle, J.F., Katsaras, J., 1999. Absence of a vestigial vapor pressure paradox. Phys. Rev. E 59, 7018-7024.
    • (1999) Phys. Rev. E , vol.59 , pp. 7018-7024
    • Nagle, J.F.1    Katsaras, J.2
  • 51
    • 0030033065 scopus 로고    scopus 로고
    • X-ray structure determination of fully hydrated Lα phase dipalmitoylphosphatidylcholine bilayers
    • Nagle, J.F., Zhang, R., Tristram-Nagle, S., Sun, W., Petrache, H.I., Suter, R.M., 1996. X-ray structure determination of fully hydrated Lα phase dipalmitoylphosphatidylcholine bilayers. Biophys. J. 70, 1419-1431.
    • (1996) Biophys. J. , vol.70 , pp. 1419-1431
    • Nagle, J.F.1    Zhang, R.2    Tristram-Nagle, S.3    Sun, W.4    Petrache, H.I.5    Suter, R.M.6
  • 52
    • 0024281314 scopus 로고
    • Micelle-vesicle transition of egg phoshatidylcholine and octyl glucoside
    • Ollivon, M., Eidelman, O., Blumenthal, R., Walter, A., 1988. Micelle-vesicle transition of egg phoshatidylcholine and octyl glucoside. Biochemistry 27, 1695-1703.
    • (1988) Biochemistry , vol.27 , pp. 1695-1703
    • Ollivon, M.1    Eidelman, O.2    Blumenthal, R.3    Walter, A.4
  • 53
    • 84862337185 scopus 로고    scopus 로고
    • Bee venom in cancer therapy
    • Oršolić, N., 2012. Bee venom in cancer therapy. Cancer Metastasis Rev. 31, 173-194.
    • (2012) Cancer Metastasis Rev. , vol.31 , pp. 173-194
    • Oršolić, N.1
  • 54
    • 36248957675 scopus 로고    scopus 로고
    • Entropy-driven softening of fluid lipid bilayers by alamethicin
    • Pabst, G., Danner, S., Podgornik, R., Katsaras, J., 2007. Entropy-driven softening of fluid lipid bilayers by alamethicin. Langmuir 23, 11705-11711.
    • (2007) Langmuir , vol.23 , pp. 11705-11711
    • Pabst, G.1    Danner, S.2    Podgornik, R.3    Katsaras, J.4
  • 56
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstruction procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100, octyl glucoside, and sodium cholate
    • Paternostre, M.-T., Roux, M., Rigaud, J.-L., 1988. Mechanisms of membrane protein insertion into liposomes during reconstruction procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100, octyl glucoside, and sodium cholate. Biochemistry 27, 2668-2677.
    • (1988) Biochemistry , vol.27 , pp. 2668-2677
    • Paternostre, M.-T.1    Roux, M.2    Rigaud, J.-L.3
  • 57
    • 0021587216 scopus 로고
    • Elastic and flexoelectric aspects of out-of-plane fluctuations in biological and model membranes
    • Petrov, A.G., Bivas, I., 1984. Elastic and flexoelectric aspects of out-of-plane fluctuations in biological and model membranes. Prog. Surf. Sci. 16, 389.
    • (1984) Prog. Surf. Sci. , vol.16 , pp. 389
    • Petrov, A.G.1    Bivas, I.2
  • 58
    • 0000863782 scopus 로고    scopus 로고
    • Bilayers of neutral lipids bear a small but significant charge
    • Pincet, F., Cribier, S., Perez, E., 1999. Bilayers of neutral lipids bear a small but significant charge. Eur. Biophys. J. 11, 127-130.
    • (1999) Eur. Biophys. J , vol.11 , pp. 127-130
    • Pincet, F.1    Cribier, S.2    Perez, E.3
  • 59
    • 46449109664 scopus 로고    scopus 로고
    • Giant unilamellar vesicle formation under physiologically relevant conditions
    • Pott, T., Bouvrais, H., Méléard, P., 2008. Giant unilamellar vesicle formation under physiologically relevant conditions. Chem. Phys. Lipids 154, 115-119.
    • (2008) Chem. Phys. Lipids , vol.154 , pp. 115-119
    • Pott, T.1    Bouvrais, H.2    Méléard, P.3
  • 60
    • 0031901414 scopus 로고    scopus 로고
    • A comparative study of the action of melittin on sphingomyelin and phosphatidylcholine bilayers
    • Pott, T., Paternostre, M.-T., Dufourc, E.J., 1998. A comparative study of the action of melittin on sphingomyelin and phosphatidylcholine bilayers. Eur. Biophys. J. 27, 237-245.
    • (1998) Eur. Biophys. J , vol.27 , pp. 237-245
    • Pott, T.1    Paternostre, M.-T.2    Dufourc, E.J.3
  • 61
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay, S.C., Condie, C.C., 1983. Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction. Biochemistry 22, 695-700.
    • (1983) Biochemistry , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 62
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • Raghuraman, H., Chattopadhyay, A., 2007. Melittin: a membrane-active peptide with diverse functions. Biosci. Rep. 27, 189-223.
    • (2007) Biosci. Rep , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 63
    • 0023682461 scopus 로고
    • Variation in hydration forces between neutral phospholipid bilayers: Evidence for hydration attraction
    • Rand, R.P., Fuller, N., Parsegian, V.A., Rau, D.C., 1988. Variation in hydration forces between neutral phospholipid bilayers: evidence for hydration attraction. Biochemistry 27, 7711-7722.
    • (1988) Biochemistry , vol.27 , pp. 7711-7722
    • Rand, R.P.1    Fuller, N.2    Parsegian, V.A.3    Rau, D.C.4
  • 64
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • Rex, S., Schwarz, G., 1998. Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles. Biochemistry 37, 2336-2345.
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 65
    • 0024591992 scopus 로고
    • Thermodynamic and kinetic studies on the association of melittin with phospholipids
    • Schwarz, G., Beschiaschvili, G., 1989. Thermodynamic and kinetic studies on the association of melittin with phospholipids. Biochim. Biophys. Acta 979, 82.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 82
    • Schwarz, G.1    Beschiaschvili, G.2
  • 66
    • 0023056958 scopus 로고
    • Thermodynamic analysis of incorporation and aggregation in a membrane: Application to the pore-forming peptide alamethicin
    • Schwarz, G., Stankowski, S., Rizzo, V., 1986. Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin. Biochim. Biophys. Acta (BBA): Biomembr. 861, 141-151.
    • (1986) Biochim. Biophys. Acta (BBA): Biomembr. , vol.861 , pp. 141-151
    • Schwarz, G.1    Stankowski, S.2    Rizzo, V.3
  • 70
    • 0018483723 scopus 로고
    • Conformational change and self-association of monomeric melittin
    • Talbot, J.C., Dufourcq, J., De Bony, J., Faucon, J.F., Lussan, C., 1979. Conformational change and self-association of monomeric melittin. FEBS Lett. 102, 191-193.
    • (1979) FEBS Lett. , vol.102 , pp. 191-193
    • Talbot, J.C.1    Dufourcq, J.2    De Bony, J.3    Faucon, J.F.4    Lussan, C.5
  • 71
    • 33947733183 scopus 로고    scopus 로고
    • Negatively cooperative binding of melittin to neutral phospholipid vesicles
    • Torrens, F., Castellano, G., Campos, A., Abad, C., 2007. Negatively cooperative binding of melittin to neutral phospholipid vesicles. J. Mol. Struct. 834-836, 216-228.
    • (2007) J. Mol. Struct. , vol.834-836 , pp. 216-228
    • Torrens, F.1    Castellano, G.2    Campos, A.3    Abad, C.4
  • 73
    • 0031824356 scopus 로고    scopus 로고
    • Structure and interactions of fully hydrated dioleoylphosphatidylcholine bilayers
    • Tristram-Nagle, S., Petrache, H.I., Nagle, J.F., 1998. Structure and interactions of fully hydrated dioleoylphosphatidylcholine bilayers. Biophys. J. 75, 917-925.
    • (1998) Biophys. J. , vol.75 , pp. 917-925
    • Tristram-Nagle, S.1    Petrache, H.I.2    Nagle, J.F.3
  • 74
    • 32344451858 scopus 로고    scopus 로고
    • Alamethicin influence on the membrane bending elasticity
    • Vitkova, V., Méléard, P., Pott, T., Bivas, I., 2006. Alamethicin influence on the membrane bending elasticity. Eur. Biophys. J. 35, 281-286.
    • (2006) Eur. Biophys. J. , vol.35 , pp. 281-286
    • Vitkova, V.1    Méléard, P.2    Pott, T.3    Bivas, I.4
  • 75
    • 58149173186 scopus 로고    scopus 로고
    • Melittin-lipid bilayer interactions and the role of cholesterol
    • Wessman, P., Strömstedt, A.A., Malmsten, M., Edwards, K., 2008. Melittin-lipid bilayer interactions and the role of cholesterol. Biophys. J. 95, 4324-4336.
    • (2008) Biophys. J. , vol.95 , pp. 4324-4336
    • Wessman, P.1    Strömstedt, A.A.2    Malmsten, M.3    Edwards, K.4
  • 76
    • 0025819980 scopus 로고
    • Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analogue of dioleoylphosphatidylcholine
    • Wiener, M.C., White, S.H., 1991. Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analogue of dioleoylphosphatidylcholine. Biochemistry 30, 6997-7008.
    • (1991) Biochemistry , vol.30 , pp. 6997-7008
    • Wiener, M.C.1    White, S.H.2
  • 77
    • 0033543167 scopus 로고    scopus 로고
    • Binding of antibacterial magainin peptides to electrically neutral membranes: Thermodynamics and structure
    • Wieprecht, T., Beyermann, M., Seelig, J., 1999. Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure. Biochemistry 38, 10377-10387.
    • (1999) Biochemistry , vol.38 , pp. 10377-10387
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 78
    • 0029022547 scopus 로고
    • X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: Diphytanoyl phosphatidylcholine with alamethicine at low concentrations
    • Wu, Y., He, K., Ludtke, S.J., Huang, H.W., 1995. X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicine at low concentrations. Biophys. J. 68, 2361-2369.
    • (1995) Biophys. J. , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 79
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., Harroun, T.A., Weiss, T.M., Ding, L., Huang, H.W., 2001. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81, 1475-1485.
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 80
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M., 2002. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.