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Volumn 370, Issue 3, 2007, Pages 459-470

Folding Amphipathic Helices Into Membranes: Amphiphilicity Trumps Hydrophobicity

Author keywords

antimicrobial peptides; hydrophobic moment; membrane proteins; peptide secondary structure; toxins

Indexed keywords

ALANINE; GLUTAMINE; LEUCINE; MEMBRANE PROTEIN;

EID: 34250195381     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.016     Document Type: Article
Times cited : (145)

References (56)
  • 1
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: a measure of the amphiphilicity of a helix
    • Eisenberg D., Weiss R.M., and Terwilliger T.C. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature 299 (1982) 371-374
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 2
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees D.C., De Antonio L., and Eisenberg D. Hydrophobic organization of membrane proteins. Science 245 (1989) 510-513
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    De Antonio, L.2    Eisenberg, D.3
  • 3
    • 12344330612 scopus 로고    scopus 로고
    • A study of the membrane-water interface region of membrane proteins
    • Granseth E., von Heijne G., and Elofsson A. A study of the membrane-water interface region of membrane proteins. J. Mol. Biol. 346 (2005) 377-385
    • (2005) J. Mol. Biol. , vol.346 , pp. 377-385
    • Granseth, E.1    von Heijne, G.2    Elofsson, A.3
  • 4
    • 12444274301 scopus 로고    scopus 로고
    • Crystal structure of the potassium channel KirBac1.1 in the closed state
    • Kuo A., Gulbis J.M., Antcliff J.F., Rahman T., Lowe E.D., Zimmer J., et al. Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300 (2003) 1922-1926
    • (2003) Science , vol.300 , pp. 1922-1926
    • Kuo, A.1    Gulbis, J.M.2    Antcliff, J.F.3    Rahman, T.4    Lowe, E.D.5    Zimmer, J.6
  • 5
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • Long S.B., Campbell E.B., and MacKinnon R. Voltage sensor of Kv1.2: Structural basis of electromechanical coupling. Science 309 (2005) 903-908
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 6
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K., Murakami S., Suzuki M., Nakagawa A., Yamashita E., Okada K., and Ito K. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127 (2006) 789-801
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 8
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • Dathe M., Wieprecht T., Nikolenko H., Handel L., Maloy W.L., MacDonald D.L., et al. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Letters 403 (1997) 208-212
    • (1997) FEBS Letters , vol.403 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    MacDonald, D.L.6
  • 9
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi A., Tarantino C., and Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur. J. Biochem. 250 (1997) 549-558
    • (1997) Eur. J. Biochem. , vol.250 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 10
    • 0030664760 scopus 로고    scopus 로고
    • Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
    • Wieprecht T., Dathe M., Krause E., Beyermann M., Maloy W.L., MacDonald D.L., and Bienert M. Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. FEBS Letters 417 (1997) 135-140
    • (1997) FEBS Letters , vol.417 , pp. 135-140
    • Wieprecht, T.1    Dathe, M.2    Krause, E.3    Beyermann, M.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 11
    • 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
  • 13
    • 0013358476 scopus 로고
    • Secondary structures of proteins and peptides in amphiphilic environments (A review)
    • Kaiser E.T., and Kézdy F.J. Secondary structures of proteins and peptides in amphiphilic environments (A review). Proc. Natl Acad. Sci. USA 80 (1983) 1137-1143
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 1137-1143
    • Kaiser, E.T.1    Kézdy, F.J.2
  • 14
    • 0021352840 scopus 로고
    • Amphiphilic secondary structure: design of peptide hormones
    • Kaiser E.T., and Kézdy F.J. Amphiphilic secondary structure: design of peptide hormones. Science 223 (1984) 249-255
    • (1984) Science , vol.223 , pp. 249-255
    • Kaiser, E.T.1    Kézdy, F.J.2
  • 15
    • 0023752362 scopus 로고
    • Conformation and orientation of regulatory peptides on lipid membranes Key to the molecular mechanish of receptor selection
    • Sargent D.F., Bean J.W., and Schwyzer R. Conformation and orientation of regulatory peptides on lipid membranes Key to the molecular mechanish of receptor selection. Biophys. Chem. 31 (1988) 183-193
    • (1988) Biophys. Chem. , vol.31 , pp. 183-193
    • Sargent, D.F.1    Bean, J.W.2    Schwyzer, R.3
  • 16
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37 (1995) 105-122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 17
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Struct. Biol. 3 (1996) 842-848
    • (1996) Nature Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 19
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann E. Bee and wasp venoms. Science 177 (1972) 314-322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 20
    • 0019871670 scopus 로고
    • Incorporation of melittin into phosphatidylcholine bilayers: study of binding and conformational changes
    • Vogel H. Incorporation of melittin into phosphatidylcholine bilayers: study of binding and conformational changes. FEBS Letters 134 (1981) 37-42
    • (1981) FEBS Letters , vol.134 , pp. 37-42
    • Vogel, H.1
  • 21
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • Kuchinka E., and Seelig J. Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation. Biochemistry 28 (1989) 4216-4221
    • (1989) Biochemistry , vol.28 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 22
    • 0025808271 scopus 로고
    • Effective charge of melittin upon interaction with POPC vesicles
    • Beschiaschvili G., and Baeuerle H.-D. Effective charge of melittin upon interaction with POPC vesicles. Biochim. Biophys. Acta 1068 (1991) 195-200
    • (1991) Biochim. Biophys. Acta , vol.1068 , pp. 195-200
    • Beschiaschvili, G.1    Baeuerle, H.-D.2
  • 23
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin
    • Ladokhin A.S., and White S.H. Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285 (1999) 1363-1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 24
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study
    • Oren Z., and Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36 (1997) 1826-1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 25
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the α-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium
    • Wieprecht T., Apostolov O., Beyermann M., and Seelig J. Thermodynamics of the α-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium. J. Mol. Biol. 294 (1999) 785-794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 26
    • 0038131038 scopus 로고    scopus 로고
    • Thermodynamics of fusion peptide-membrane interactions
    • Li Y., Han X., and Tamm L.K. Thermodynamics of fusion peptide-membrane interactions. Biochemistry 42 (2003) 7245-7251
    • (2003) Biochemistry , vol.42 , pp. 7245-7251
    • Li, Y.1    Han, X.2    Tamm, L.K.3
  • 27
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe M., Schümann M., Wieprecht T., Winkler A., Beyermann M., Krause E., et al. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35 (1996) 12612-12622
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schümann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6
  • 28
    • 0035827137 scopus 로고    scopus 로고
    • Protein chemistry at membrane interfaces: non-additivity of electrostatic and hydrophobic interactions
    • Ladokhin A.S., and White S.H. Protein chemistry at membrane interfaces: non-additivity of electrostatic and hydrophobic interactions. J. Mol. Biol. 309 (2001) 543-552
    • (2001) J. Mol. Biol. , vol.309 , pp. 543-552
    • Ladokhin, A.S.1    White, S.H.2
  • 30
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struc. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struc. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 31
    • 2442442435 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of a designed helical peptide
    • Ladokhin A.S., and White S.H. Interfacial folding and membrane insertion of a designed helical peptide. Biochemistry 43 (2004) 5782-5791
    • (2004) Biochemistry , vol.43 , pp. 5782-5791
    • Ladokhin, A.S.1    White, S.H.2
  • 32
    • 24944516963 scopus 로고    scopus 로고
    • An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces
    • Hristova K., and White S.H. An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces. Biochemistry 44 (2005) 12614-12619
    • (2005) Biochemistry , vol.44 , pp. 12614-12619
    • Hristova, K.1    White, S.H.2
  • 33
    • 0031042309 scopus 로고    scopus 로고
    • Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol
    • Hirota N., Mizuno K., and Goto Y. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6 (1997) 416-421
    • (1997) Protein Sci. , vol.6 , pp. 416-421
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 34
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins
    • Hirota N., Mizuno K., and Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275 (1998) 365-378
    • (1998) J. Mol. Biol. , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 35
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin A.S., Jayasinghe S., and White S.H. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?. Anal. Biochem. 285 (2000) 235-245
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 36
    • 0034581611 scopus 로고    scopus 로고
    • The relationship between sequence and structure in elementary folding units
    • Serrano L. The relationship between sequence and structure in elementary folding units. Adv. Protein Chem. 53 (2000) 49-85
    • (2000) Adv. Protein Chem. , vol.53 , pp. 49-85
    • Serrano, L.1
  • 37
    • 0027298784 scopus 로고
    • Aromatic side-chain contribution to the far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
    • Chakrabartty A., Kortemme T., Padmanabhan S., and Baldwin R.L. Aromatic side-chain contribution to the far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32 (1993) 5560-5565
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 38
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T., Kim H., Bihlmaier K., Lundin C., Boekel J., Andersson H., et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433 (2005) 377-381
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Bihlmaier, K.3    Lundin, C.4    Boekel, J.5    Andersson, H.6
  • 39
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: determining the energetics of peptide-bilayer interactions
    • White S.H., Wimley W.C., Ladokhin A.S., and Hristova K. Protein folding in membranes: determining the energetics of peptide-bilayer interactions. Methods Enzymol. 295 (1998) 62-87
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 40
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl C.A., Chakrabartty A., and Baldwin R.L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5 (1996) 2623-2637
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 41
    • 0028569692 scopus 로고
    • Tests for helix-stabilizing interactions between various non-polar side chains in alanine-based peptides
    • Padmanabhan S., and Baldwin R.L. Tests for helix-stabilizing interactions between various non-polar side chains in alanine-based peptides. Protein Sci. 3 (1994) 1992-1997
    • (1994) Protein Sci. , vol.3 , pp. 1992-1997
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 42
    • 0027960477 scopus 로고
    • Discovering structural correlations in α-helices
    • Klingler T.M., and Brutlag D.L. Discovering structural correlations in α-helices. Protein Sci. 3 (1994) 1847-1857
    • (1994) Protein Sci. , vol.3 , pp. 1847-1857
    • Klingler, T.M.1    Brutlag, D.L.2
  • 43
    • 0029077857 scopus 로고
    • Interactions between hydrophobic side chains within α-helices
    • Creamer T.P., and Rose G.D. Interactions between hydrophobic side chains within α-helices. Protein Sci. 4 (1995) 1305-1314
    • (1995) Protein Sci. , vol.4 , pp. 1305-1314
    • Creamer, T.P.1    Rose, G.D.2
  • 44
    • 0032511138 scopus 로고    scopus 로고
    • Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins
    • Avbelj F., and Fele L. Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins. J. Mol. Biol. 279 (1998) 665-684
    • (1998) J. Mol. Biol. , vol.279 , pp. 665-684
    • Avbelj, F.1    Fele, L.2
  • 45
    • 0037007465 scopus 로고    scopus 로고
    • Origin of the different strengths of the (i,i+4) and (i,i+3) leucine pair interactions in helices
    • Luo P., and Baldwin R.L. Origin of the different strengths of the (i,i+4) and (i,i+3) leucine pair interactions in helices. Biophys. Chem. 96 (2002) 103-108
    • (2002) Biophys. Chem. , vol.96 , pp. 103-108
    • Luo, P.1    Baldwin, R.L.2
  • 46
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Muñoz V., and Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245 (1995) 275-296
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 47
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • Muñoz V., and Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245 (1995) 297-308
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 48
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz V., and Serrano L. Development of the multiple sequence approximation within the AGADIR model of α-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 41 (1997) 495-509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 49
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix E., Viguera A.R., and Serrano L. Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J. Mol. Biol. 284 (1998) 173-191
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 52
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer L.D., Hope M.J., and 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
  • 53
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen Y.-H., Yang J.T., and Chau K.H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13 (1974) 3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 54
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg D., Weiss R.M., and Terwilliger T.C. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl Acad. Sci. USA 81 (1984) 140-144
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 55
    • 33751230498 scopus 로고    scopus 로고
    • Diffraction-based density restraints for membrane and membrane/protein molecular dynamics simulations
    • Benz R.W., Nanda H., Castro-Román F., White S.H., and Tobias D.J. Diffraction-based density restraints for membrane and membrane/protein molecular dynamics simulations. Biophys. J. 91 (2006) 3617-3629
    • (2006) Biophys. J. , vol.91 , pp. 3617-3629
    • Benz, R.W.1    Nanda, H.2    Castro-Román, F.3    White, S.H.4    Tobias, D.J.5


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