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Volumn 85, Issue 2-3, 2000, Pages 209-228

A Pro→Ala substitution in melittin affects self-association, membrane binding and pore-formation kinetics due to changes in structural and electrostatic properties

Author keywords

Aggregation; Binding isotherm; Charge screening; Peptide induced leakage; Proline14; Ala 14 melittin

Indexed keywords

MELITTIN;

EID: 0033939053     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00121-6     Document Type: Article
Times cited : (32)

References (55)
  • 1
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil K.T., Degrado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:1990;646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 2
    • 0001810769 scopus 로고
    • Prediction of protein structure and the principles of protein conformation
    • G.D. Fasman. New York: Plenum Press
    • Richardson J.S., Richardson D.C. Prediction of protein structure and the principles of protein conformation. Fasman G.D. Principles and Patterns of Protein Conformation. 1989;1-98 Plenum Press, New York.
    • (1989) Principles and Patterns of Protein Conformation , pp. 1-98
    • Richardson, J.S.1    Richardson, D.C.2
  • 3
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamical role?
    • Williams K.A., Deber C.M. Proline residues in transmembrane helices: structural or dynamical role? Biochemistry. 30:1991;8919-8923.
    • (1991) Biochemistry , vol.30 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 5
    • 0030015420 scopus 로고    scopus 로고
    • α-helical, but not β-sheet, propensity of proline is determined by peptide environment
    • Li S.-C., Goto N.K., Williams K.A., Deber C.M. α-helical, but not β-sheet, propensity of proline is determined by peptide environment. Proc. Natl. Acad. Sci. USA. 93:1996;6676-6681.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6676-6681
    • Li, S.-C.1    Goto, N.K.2    Williams, K.A.3    Deber, C.M.4
  • 6
    • 0028889187 scopus 로고
    • Functional consequences of proline mutations in the putative transmembrane segments 6 and 10 of the glucose transporter GLUT1
    • Wellner M., Monden I., Mueckler M.M., Keller K. Functional consequences of proline mutations in the putative transmembrane segments 6 and 10 of the glucose transporter GLUT1. Eur. J. Biochem. 227:1995;454-458.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 454-458
    • Wellner, M.1    Monden, I.2    Mueckler, M.M.3    Keller, K.4
  • 7
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandl C.J., Deber C.M. Hypothesis about the function of membrane-buried proline residues in transport proteins. Proc. Natl. Acad. Sci. USA. 83:1986;917-921.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 917-921
    • Brandl, C.J.1    Deber, C.M.2
  • 9
    • 0022497150 scopus 로고
    • Interactions between membranes and cytolytic peptides
    • Bernheimer A.W., Rudy B. Interactions between membranes and cytolytic peptides. Biochim. Biophys. Acta. 864:1986;123-141.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 123-141
    • Bernheimer, A.W.1    Rudy, B.2
  • 10
    • 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
  • 11
    • 0027254408 scopus 로고
    • Possible mechanism of action of cobra snake venom cardiotoxins and bee venom melittin
    • Fletcher J.E., Jiang M.S. Possible mechanism of action of cobra snake venom cardiotoxins and bee venom melittin. Toxicon. 31:1993;669-695.
    • (1993) Toxicon , vol.31 , pp. 669-695
    • Fletcher, J.E.1    Jiang, M.S.2
  • 12
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:1997;197-211.
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 15
    • 0026079128 scopus 로고
    • Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced by melittin and [Ala-14]melittin
    • Dempsey C.E., Sternberg B. Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced by melittin and [Ala-14]melittin. Biochim. Biophys. Acta. 1061:1991;175-184.
    • (1991) Biochim. Biophys. Acta , vol.1061 , pp. 175-184
    • Dempsey, C.E.1    Sternberg, B.2
  • 16
    • 0026718141 scopus 로고
    • Quantitation of the effects of an internal proline residue on individual hydrogen bond stabilities in an α-helix: PH-dependent amide exchange in melittin and [Ala-14]melittin
    • Dempsey C.E. Quantitation of the effects of an internal proline residue on individual hydrogen bond stabilities in an α-helix: pH-dependent amide exchange in melittin and [Ala-14]melittin. Biochemistry. 31:1992;4705-4712.
    • (1992) Biochemistry , vol.31 , pp. 4705-4712
    • Dempsey, C.E.1
  • 17
    • 0029847827 scopus 로고    scopus 로고
    • Protection by chlorpromazine, albumin and bivalent cations against haemolysis induced by melittin, [Ala-14]melittin and whole bee venom
    • Rudenko S.V., Nipot E.E. Protection by chlorpromazine, albumin and bivalent cations against haemolysis induced by melittin, [Ala-14]melittin and whole bee venom. Biochem. J. 317:1996;747-754.
    • (1996) Biochem. J. , vol.317 , pp. 747-754
    • Rudenko, S.V.1    Nipot, E.E.2
  • 18
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay S.C., Condie C.C. Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction. Biochemistry. 22:1983;695-700.
    • (1983) Biochemistry , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 19
    • 0021187451 scopus 로고
    • Weak acid-induced release of liposome-encapsulated carboxyfluorescein
    • Barbet J., Machy P., Truneh A., Leserman L.D. Weak acid-induced release of liposome-encapsulated carboxyfluorescein. Biochim. Biophys. Acta. 772:1984;347-356.
    • (1984) Biochim. Biophys. Acta , vol.772 , pp. 347-356
    • Barbet, J.1    Machy, P.2    Truneh, A.3    Leserman, L.D.4
  • 20
    • 0022549772 scopus 로고
    • Molecular mobility and nucleocytoplasmic flux in heptoma cells
    • Lang I., Scholz M., Peters R. Molecular mobility and nucleocytoplasmic flux in heptoma cells. J. Cell Biol. 102:1986;1183-1190.
    • (1986) J. Cell Biol. , vol.102 , pp. 1183-1190
    • Lang, I.1    Scholz, M.2    Peters, R.3
  • 21
    • 0023709016 scopus 로고
    • Study of the translational diffusion of macromolecules in beads of gel chromatography by the FRAP method
    • Poitevin E., Wahl P. Study of the translational diffusion of macromolecules in beads of gel chromatography by the FRAP method. Biophys. Chem. 31:1988;247-258.
    • (1988) Biophys. Chem. , vol.31 , pp. 247-258
    • Poitevin, E.1    Wahl, P.2
  • 22
    • 0030049701 scopus 로고    scopus 로고
    • Pore formation induced by the peptide melittin in different lipid vesicle membranes
    • Rex S. Pore formation induced by the peptide melittin in different lipid vesicle membranes. Biophys. Chem. 58:1996;75-85.
    • (1996) Biophys. Chem. , vol.58 , pp. 75-85
    • Rex, S.1
  • 23
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin induced leakage mechanism of lipid vesicles
    • Rex S., Schwarz G. Quantitative studies on the melittin induced leakage mechanism of lipid vesicles. Biochemistry. 37:1998;2336-2345.
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 25
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer L.D., Hope M.J., Cullis P.R. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta. 858:1986;161-168.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 26
    • 50549164858 scopus 로고
    • A rapid and sensitive sub-micro phosphorus determination
    • Böttcher C.F.J., vanGent C.M., Pries C. A rapid and sensitive sub-micro phosphorus determination. Anal. Chim. Acta. 24:1961;203-204.
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, C.F.J.1    Vangent, C.M.2    Pries, C.3
  • 27
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen Y.-H., Yang J.T., Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 11:1972;4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.-H.1    Yang, J.T.2    Martinez, H.M.3
  • 28
    • 0019751507 scopus 로고
    • Protein determination in membrane and lipoprotein samples: Manual and automated procedures
    • Markwell M.A.K., Haas S.M., Tolbert N.E., Bieber L.L. Protein determination in membrane and lipoprotein samples: manual and automated procedures. Methods Enzymol. 72:1981;296-303.
    • (1981) Methods Enzymol. , vol.72 , pp. 296-303
    • Markwell, M.A.K.1    Haas, S.M.2    Tolbert, N.E.3    Bieber, L.L.4
  • 29
    • 0032473539 scopus 로고    scopus 로고
    • Peptide-liposome association. A critical examination with mastoparan-X
    • Hellmann N., Schwarz G. Peptide-liposome association. A critical examination with mastoparan-X. Biochim. Biophys. Acta. 1369:1998;267-277.
    • (1998) Biochim. Biophys. Acta , vol.1369 , pp. 267-277
    • Hellmann, N.1    Schwarz, G.2
  • 30
    • 0023441012 scopus 로고
    • Incorporation kinetics in a membrane studied with the pore-forming peptide alamethicin
    • Schwarz G., Gerke H., Rizzo V., Stankowski S. Incorporation kinetics in a membrane studied with the pore-forming peptide alamethicin. Biophys. J. 52:1987;685-692.
    • (1987) Biophys. J. , vol.52 , pp. 685-692
    • Schwarz, G.1    Gerke, H.2    Rizzo, V.3    Stankowski, S.4
  • 31
    • 0030023552 scopus 로고    scopus 로고
    • Electrical interactions of membrane active peptides at lipid/water interfaces
    • Schwarz G. Electrical interactions of membrane active peptides at lipid/water interfaces. Biophys. Chem. 58:1996;67-73.
    • (1996) Biophys. Chem. , vol.58 , pp. 67-73
    • Schwarz, G.1
  • 32
    • 0029099270 scopus 로고
    • Pore kinetics reflected in the dequenching of a lipid vesicle entrapped fluorescent dye
    • Schwarz G., Arbuzova A. Pore kinetics reflected in the dequenching of a lipid vesicle entrapped fluorescent dye. Biochim. Biophys. Acta. 1239:1995;51-57.
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 51-57
    • Schwarz, G.1    Arbuzova, A.2
  • 33
    • 0026910992 scopus 로고
    • Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength, and temperature-models for protein folding and halophilic proteins
    • Ramalingam K., Aimoto S., Bello J. Conformational studies of anionic melittin analogues: effect of peptide concentration, pH, ionic strength, and temperature-models for protein folding and halophilic proteins. Biopolymers. 32:1992;981-992.
    • (1992) Biopolymers , vol.32 , pp. 981-992
    • Ramalingam, K.1    Aimoto, S.2    Bello, J.3
  • 34
    • 0028883162 scopus 로고
    • The role of amphipathicity in the folding self-association and biological activity of multiple subunit small proteins
    • Pérez-Payá E., Houghten R.A., Blondelle S.E. The role of amphipathicity in the folding self-association and biological activity of multiple subunit small proteins. J. Biol. Chem. 20:1995;1048-1056.
    • (1995) J. Biol. Chem. , vol.20 , pp. 1048-1056
    • Pérez-Payá, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 35
    • 0020473234 scopus 로고
    • Conformation and aggregation of melittin: Dependence on pH and concentration
    • Bello J., Bello H.R., Granados E. Conformation and aggregation of melittin: dependence on pH and concentration. Biochemistry. 21:1982;461-465.
    • (1982) Biochemistry , vol.21 , pp. 461-465
    • Bello, J.1    Bello, H.R.2    Granados, E.3
  • 36
    • 0026602028 scopus 로고
    • Mechanism of the conformational transition of melittin
    • Goto Y., Hagihara Y. Mechanism of the conformational transition of melittin. Biochemistry. 31:1992;732-738.
    • (1992) Biochemistry , vol.31 , pp. 732-738
    • Goto, Y.1    Hagihara, Y.2
  • 37
    • 0023504970 scopus 로고
    • Structure-function analysis of proteins through the design synthesis and study of peptide models
    • Taylor F.W., Kaiser E.T. Structure-function analysis of proteins through the design synthesis and study of peptide models. Methods Enzymol. 154:1987;473-498.
    • (1987) Methods Enzymol. , vol.154 , pp. 473-498
    • Taylor, F.W.1    Kaiser, E.T.2
  • 38
    • 0024591992 scopus 로고
    • Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer
    • Schwarz G., Beschiaschvili G. Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer. Biochim. Biophys. Acta. 979:1989;82-90.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 82-90
    • Schwarz, G.1    Beschiaschvili, G.2
  • 39
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg J., Blumenthal R., Sarkar D.P., Curran M., Morris S.J. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. J. Cell Biol. 127:1994;1885-1894.
    • (1994) J. Cell Biol. , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5
  • 40
    • 0026607062 scopus 로고
    • Kinetics of pore-mediated release of marker molecules from liposomes or cells
    • Schwarz G., Robert C. Kinetics of pore-mediated release of marker molecules from liposomes or cells. Biophys. Chem. 42:1992;291-296.
    • (1992) Biophys. Chem. , vol.42 , pp. 291-296
    • Schwarz, G.1    Robert, C.2
  • 41
    • 0000368218 scopus 로고    scopus 로고
    • Pore kinetics of mastoparan peptides in large unilamellar lipid vesicles
    • Arbuzova A., Schwarz G. Pore kinetics of mastoparan peptides in large unilamellar lipid vesicles. Prog. Colloid Polym. Sci. 100:1996;345-350.
    • (1996) Prog. Colloid Polym. Sci. , vol.100 , pp. 345-350
    • Arbuzova, A.1    Schwarz, G.2
  • 42
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47:1978;45-148.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 43
    • 0018784022 scopus 로고
    • The structure of melittin in lipid bilayer membranes
    • Drake A.F., Hider R.C. The structure of melittin in lipid bilayer membranes. Biochim. Biophys. Acta. 555:1979;371-373.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 371-373
    • Drake, A.F.1    Hider, R.C.2
  • 44
    • 0018487558 scopus 로고
    • The self-association of melittin and its binding to lipids
    • Faucon J.F., Dufourcq J., Lussan C. The self-association of melittin and its binding to lipids. FEBS Lett. 102:1979;187-190.
    • (1979) FEBS Lett. , vol.102 , pp. 187-190
    • Faucon, J.F.1    Dufourcq, J.2    Lussan, C.3
  • 46
    • 0026470007 scopus 로고
    • Charge repulsion in the conformational stability of melittin
    • Hagihara Y., Kataoka M., Aimoto S., Goto Y. Charge repulsion in the conformational stability of melittin. Biochemistry. 31:1992;11908-11914.
    • (1992) Biochemistry , vol.31 , pp. 11908-11914
    • Hagihara, Y.1    Kataoka, M.2    Aimoto, S.3    Goto, Y.4
  • 47
    • 0024471945 scopus 로고
    • 13C-labeled synthetic melittin and melittin analogues in isotropic solvents by circular dichroism fluorescence and NMR spectroscopy
    • 13C-labeled synthetic melittin and melittin analogues in isotropic solvents by circular dichroism fluorescence and NMR spectroscopy. Biochemistry. 28:1989;8614-8623.
    • (1989) Biochemistry , vol.28 , pp. 8614-8623
    • Weaver, A.J.1    Kemple, M.D.2    Prendergast, F.G.3
  • 48
    • 0018483723 scopus 로고
    • Conformational change and self association of monomeric melittin
    • Talbot J.C., Dufourcq J., deBony J., Faucon J.F., Lussan C. Conformational change and self association of monomeric melittin. FEBS Lett. 102:1979;191-193.
    • (1979) FEBS Lett. , vol.102 , pp. 191-193
    • Talbot, J.C.1    Dufourcq, J.2    Debony, J.3    Faucon, J.F.4    Lussan, C.5
  • 49
    • 0027058921 scopus 로고
    • A synthetic analogue of melittin aggregates in large oligomers
    • John E., Jähnig F. A synthetic analogue of melittin aggregates in large oligomers. Biophys. J. 63:1992;1536-1543.
    • (1992) Biophys. J. , vol.63 , pp. 1536-1543
    • John, E.1    Jähnig, F.2
  • 50
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • Vogel H., Jähnig F. The structure of melittin in membranes. Biophys. J. 50:1986;573-582.
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jähnig, F.2
  • 51
    • 0028344411 scopus 로고
    • Determination of the secondary structure of selected melittin analogues with different haemolytic activities
    • Pérez-Payá E., Houghten R.A., Blondelle S.E. Determination of the secondary structure of selected melittin analogues with different haemolytic activities. Biochem. J. 299:1994;587-591.
    • (1994) Biochem. J. , vol.299 , pp. 587-591
    • Pérez-Payá, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 52
    • 0028022950 scopus 로고
    • Vesicle-bound conformation of melittin: Transferred nuclear overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles
    • Okada A., Wakamatsu K., Miyazawa T., Higashijima T. Vesicle-bound conformation of melittin: transferred nuclear overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles. Biochemistry. 33:1994;9438-9446.
    • (1994) Biochemistry , vol.33 , pp. 9438-9446
    • Okada, A.1    Wakamatsu, K.2    Miyazawa, T.3    Higashijima, T.4
  • 53
    • 0030971376 scopus 로고    scopus 로고
    • Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin
    • Ladokhin A.S., Selsted M.E., White S.H. Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin. Biophys. J. 72:1997;1762-1766.
    • (1997) Biophys. J. , vol.72 , pp. 1762-1766
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 54
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki K., Yoneyama S., Miyajima K. Pore formation and translocation of melittin. Biophys. J. 73:1997;831-838.
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 55
    • 0026746013 scopus 로고
    • Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ
    • Dempsey C.E., Butler G.S. Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ. Biochemistry. 31:1992;11973-11977.
    • (1992) Biochemistry , vol.31 , pp. 11973-11977
    • Dempsey, C.E.1    Butler, G.S.2


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