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Volumn 46, Issue 4, 2007, Pages 1042-1054

Studies of the minimum hydrophobicity of α-helical peptides required to maintain a stable transmembrane association with phospholipid bilayer membranes

Author keywords

[No Author keywords available]

Indexed keywords

AQUEOUS PHASE; LIPID BILAYER MEMBRANES; SELF-AGGREGATION; TRANSMEMBRANE PEPTIDES;

EID: 33846621039     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061891b     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 0037093905 scopus 로고    scopus 로고
    • Mechanisms of the interaction of α-helical transmembrane peptides with phospholipid bilayers
    • Lewis, R. N. A. H., Zhang, Y. P., Liu, F., and McElhaney, R. N. (2002) Mechanisms of the interaction of α-helical transmembrane peptides with phospholipid bilayers, Bioelectrochemistry 56, 135-140.
    • (2002) Bioelectrochemistry , vol.56 , pp. 135-140
    • Lewis, R.N.A.H.1    Zhang, Y.P.2    Liu, F.3    McElhaney, R.N.4
  • 2
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R. R., and Killian, J. A. (2003) Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring, Mol. Membr. Biol. 20, 271-284.
    • (2003) Mol. Membr. Biol , vol.20 , pp. 271-284
    • de Planque, M.R.R.1    Killian, J.A.2
  • 3
    • 0001006658 scopus 로고
    • Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure
    • Davis, J. H., Clare, D. M., Hodges, R. S., and Bloom, M. (1983) Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure, Biochemistry 22, 5298-5305.
    • (1983) Biochemistry , vol.22 , pp. 5298-5305
    • Davis, J.H.1    Clare, D.M.2    Hodges, R.S.3    Bloom, M.4
  • 4
    • 0026482964 scopus 로고
    • FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins
    • Zhang, Y. P., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (1992) FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins, Biochemistry 31, 11572-11578.
    • (1992) Biochemistry , vol.31 , pp. 11572-11578
    • Zhang, Y.P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 5
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • Zhang, Y. P., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (1992) Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies, Biochemistry 31, 11579-11588.
    • (1992) Biochemistry , vol.31 , pp. 11579-11588
    • Zhang, Y.P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 6
    • 0028879250 scopus 로고
    • The infrared dichroism of transmembrane helical polypeptides
    • Axelsen, P. H., Kaufman, P. H., McElhaney, R. N., and Lewis, R. N. A. H. (1995) The infrared dichroism of transmembrane helical polypeptides, Biophys. J. 69, 2770-2781.
    • (1995) Biophys. J , vol.69 , pp. 2770-2781
    • Axelsen, P.H.1    Kaufman, P.H.2    McElhaney, R.N.3    Lewis, R.N.A.H.4
  • 7
    • 0024968216 scopus 로고
    • Orientation of α-helical peptides in a lipid bilayer
    • Huschilt, J. C., Millman, B. M., and Davis, J. H. (1989) Orientation of α-helical peptides in a lipid bilayer, Biochim. Biophys. Acta 979, 139-141.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 139-141
    • Huschilt, J.C.1    Millman, B.M.2    Davis, J.H.3
  • 8
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J., and Holloway, P. W. (1990) Quenching of tryptophan fluorescence by brominated phospholipid, Biochemistry 29, 9638-9643.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 9
    • 0000616967 scopus 로고
    • Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy
    • Huschilt, J. C., Hodges, R. S., and Davis, J. H. (1985) Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy, Biochemistry 24, 1377-1386.
    • (1985) Biochemistry , vol.24 , pp. 1377-1386
    • Huschilt, J.C.1    Hodges, R.S.2    Davis, J.H.3
  • 10
    • 0022399766 scopus 로고
    • Simultaneous modeling of phase and calorimetric behavior in an amphiphilic peptide/phospholipid model membrane
    • Morrow, M. R., Huschilt, J. C., and Davis, J. H. (1985) Simultaneous modeling of phase and calorimetric behavior in an amphiphilic peptide/phospholipid model membrane, Biochemistry 24, 5396-5406.
    • (1985) Biochemistry , vol.24 , pp. 5396-5406
    • Morrow, M.R.1    Huschilt, J.C.2    Davis, J.H.3
  • 11
    • 0028941129 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • Zhang, Y.-P., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (1995) Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies, Biophys. J. 68, 847-857.
    • (1995) Biophys. J , vol.68 , pp. 847-857
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 13
    • 0032478081 scopus 로고    scopus 로고
    • Molecular organization and dynamics of 1-palmitoyl-2-oleoyl-phosphatidylcholine bilayers containing a transmembrane α-helical peptide
    • Subczynski, W. K., Lewis, R. N. A. H., McElhaney, R. N., Hodges, R. S., Hyde, J. S., and Kusumi, A. (1998) Molecular organization and dynamics of 1-palmitoyl-2-oleoyl-phosphatidylcholine bilayers containing a transmembrane α-helical peptide, Biochemistry 37, 3156-3164.
    • (1998) Biochemistry , vol.37 , pp. 3156-3164
    • Subczynski, W.K.1    Lewis, R.N.A.H.2    McElhaney, R.N.3    Hodges, R.S.4    Hyde, J.S.5    Kusumi, A.6
  • 14
    • 0037162409 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers
    • Liu, F., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (2002) Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers, Biochemistry 41, 9197-9207.
    • (2002) Biochemistry , vol.41 , pp. 9197-9207
    • Liu, F.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 15
    • 16644377766 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interactions with phosphatidylethanolamine bilayers
    • Liu, F., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (2004) Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interactions with phosphatidylethanolamine bilayers, Biophys. J. 87, 2470-2482.
    • (2004) Biophys. J , vol.87 , pp. 2470-2482
    • Liu, F.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 16
    • 1642279990 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interactions with phosphatidylglycerol bilayers
    • Liu, F., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (2004) Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interactions with phosphatidylglycerol bilayers, Biochemistry 43, 3679-3687.
    • (2004) Biochemistry , vol.43 , pp. 3679-3687
    • Liu, F.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 17
    • 0035936573 scopus 로고    scopus 로고
    • 31P NMR spectroscopic study of the effect of transmembrane α-helical peptides on the lamellar/reversed hexagonal phase transition of phosphatidylethanolamine model membranes
    • 31P NMR spectroscopic study of the effect of transmembrane α-helical peptides on the lamellar/reversed hexagonal phase transition of phosphatidylethanolamine model membranes, Biochemistry 40, 760-768.
    • (2001) Biochemistry , vol.40 , pp. 760-768
    • Liu, F.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 20
    • 0035831154 scopus 로고    scopus 로고
    • 2H-nuclear magnetic resonance and Fourier transform infrared spectroscopic studies of the effects of transmembrane α-helical peptides on the organization of phosphatidylcholine bilayers
    • 2H-nuclear magnetic resonance and Fourier transform infrared spectroscopic studies of the effects of transmembrane α-helical peptides on the organization of phosphatidylcholine bilayers, Biochim. Biophys. Acta 1511, 60-73.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 60-73
    • Pare, C.1    Lafleur, M.2    Liu, R.3    Lewis, R.N.A.H.4    McElhaney, R.N.5
  • 22
    • 0344406989 scopus 로고    scopus 로고
    • Molecular dynamics of 1-palmitoyl-2- oleoylphosphatidylcholine membranes containing transmembrane α-helical peptides with alternating leucine and alanine residues
    • Subczynski, W. K., Pasenkiewicz-Gierula, M., McElhaney, R. N., Hyde, J. S., and Kusumi, A. (2003) Molecular dynamics of 1-palmitoyl-2- oleoylphosphatidylcholine membranes containing transmembrane α-helical peptides with alternating leucine and alanine residues, Biochemistry 42, 3939-3948.
    • (2003) Biochemistry , vol.42 , pp. 3939-3948
    • Subczynski, W.K.1    Pasenkiewicz-Gierula, M.2    McElhaney, R.N.3    Hyde, J.S.4    Kusumi, A.5
  • 24
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Liu, P. Z., and Baldwin, R. L. (1997) Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water, Biochemistry 36, 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Liu, P.Z.1    Baldwin, R.L.2
  • 25
    • 0038265111 scopus 로고    scopus 로고
    • A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography
    • Lee, D. J., Mant, C. T., and Hodges, R. S. (2003) A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography, J. Biol. Chem. 278, 22918-22927.
    • (2003) J. Biol. Chem , vol.278 , pp. 22918-22927
    • Lee, D.J.1    Mant, C.T.2    Hodges, R.S.3
  • 26
    • 0043135171 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization of amphipathic α-helical peptides
    • Mant, C. T., Chen, Y., and Hodges, R. S. (2003) Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization of amphipathic α-helical peptides, J. Chromatogr., A 1009, 29-43.
    • (2003) J. Chromatogr., A , vol.1009 , pp. 29-43
    • Mant, C.T.1    Chen, Y.2    Hodges, R.S.3
  • 27
    • 0042634260 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography. II. Monitoring of folding and stability of two-stranded α-helical coiled-coils
    • Mant, C. T., Tripet, B., and Hodges, R. S. (2003) Temperature profiling of polypeptides in reversed-phase liquid chromatography. II. Monitoring of folding and stability of two-stranded α-helical coiled-coils, J. Chromatogr., A 1009, 45-59.
    • (2003) J. Chromatogr., A , vol.1009 , pp. 45-59
    • Mant, C.T.1    Tripet, B.2    Hodges, R.S.3
  • 28
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces, Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 29
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability. Physical principles
    • White, S. H., and Wimley, W. C. (1999) Membrane protein folding and stability. Physical principles, Annu. Rev. Biophys. Biomol. Struct. 28, 319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 31
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L. K., and Tatulian, S. A. (1997) Infrared spectroscopy of proteins and peptides in lipid bilayers, Q. Rev. Biophys. 30, 365-429.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 32
    • 0016290132 scopus 로고
    • Intensities and other spectral parameters of infrared amide bands of polypeptides in α-helical form
    • Chirgadzee, Y. N., and Brazhnikov, E. V. (1974) Intensities and other spectral parameters of infrared amide bands of polypeptides in α-helical form, Biopolymers 13, 1701-1712.
    • (1974) Biopolymers , vol.13 , pp. 1701-1712
    • Chirgadzee, Y.N.1    Brazhnikov, E.V.2
  • 33
    • 0032213021 scopus 로고    scopus 로고
    • The structure and organization of phospholipid bilayers as revealed by infrared spectroscopy
    • Lewis, R. N. A. H., and McElhaney, R. N. (1998) The structure and organization of phospholipid bilayers as revealed by infrared spectroscopy, Chem. Phys. Lipids 96, 9-21.
    • (1998) Chem. Phys. Lipids , vol.96 , pp. 9-21
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 34
    • 14544295414 scopus 로고    scopus 로고
    • Vibrational Spectroscopy of lipids
    • Chalmers, J. M, and Griffith, P. R, Eds, John Wiley and Sons, Chichester, England
    • Lewis, R. N. A. H., and McElhaney, R. N. (2002) Vibrational Spectroscopy of lipids, in Handbook of Vibrational Spectroscopy (Chalmers, J. M., and Griffith, P. R., Eds.) Vol. 5, pp 3447-3464, John Wiley and Sons, Chichester, England.
    • (2002) Handbook of Vibrational Spectroscopy , vol.5 , pp. 3447-3464
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 35
    • 0027995873 scopus 로고
    • α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix
    • Zhou, N. E., Monera, O. D., Kay, C. M., and Hodges, R. S. (1994) α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix, Protein Pept. Lett. 1, 114-119.
    • (1994) Protein Pept. Lett , vol.1 , pp. 114-119
    • Zhou, N.E.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4
  • 36
    • 0029361842 scopus 로고
    • Relationship of sidechain hydrophobicity and α-helical propensity on the stability of the single-stranded amphipathic α-helix
    • Monera, O. D., Serada, T. J., Zhou, N. E., Kay, C. M., and Hodges, R. S. (1995) Relationship of sidechain hydrophobicity and α-helical propensity on the stability of the single-stranded amphipathic α-helix, J. Pept. Sci. 1, 319-329.
    • (1995) J. Pept. Sci , vol.1 , pp. 319-329
    • Monera, O.D.1    Serada, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 37
    • 0028458257 scopus 로고
    • A measure of helical propensity for amino acids in membrane environments
    • Lis, S.-C., and Deber, C. M. (1994) A measure of helical propensity for amino acids in membrane environments, Nat. Struct. Biol. 1, 368-373.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 368-373
    • Lis, S.-C.1    Deber, C.M.2
  • 38
    • 0029153215 scopus 로고
    • Peptides in membranes α-helicity and hydrophobicity
    • Deber, C. M., and Li, S.-C. (1995) Peptides in membranes α-helicity and hydrophobicity, Biopolymers 37, 295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 39
    • 0032508664 scopus 로고    scopus 로고
    • Uncoupling hydrophobicity and helicity in transmembrane segments: α-Helical propensities of the amino acids in non-polar environments
    • Liu, L.-P., and Deber, C. M. (1998) Uncoupling hydrophobicity and helicity in transmembrane segments: α-Helical propensities of the amino acids in non-polar environments, J. Biol. Chem. 273, 23645-23648.
    • (1998) J. Biol. Chem , vol.273 , pp. 23645-23648
    • Liu, L.-P.1    Deber, C.M.2
  • 40
    • 0031555018 scopus 로고    scopus 로고
    • Secondary structure induction in aqueous vs. membrane-like environments
    • Blondelle, S. E., Forood, B., Houghten, R. A., and Perez-Paya, E. (1997) Secondary structure induction in aqueous vs. membrane-like environments, Biopolymers 42, 489-498.
    • (1997) Biopolymers , vol.42 , pp. 489-498
    • Blondelle, S.E.1    Forood, B.2    Houghten, R.A.3    Perez-Paya, E.4
  • 41
    • 0028211273 scopus 로고
    • A model approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., Taylor, W. R., and Thorton, J. M. (1994) A model approach to the prediction of all-helical membrane protein structure and topology, Biochemistry 33, 3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thorton, J.M.3
  • 42
    • 0027499143 scopus 로고
    • Nonrandom distribution of amino acid in the transmembrane segments of human type-I single span membrane proteins
    • Landolt-Marticorena, C., Williams, K. A., Deber, C. M., and Reithmeier, R. A. F. (1993) Nonrandom distribution of amino acid in the transmembrane segments of human type-I single span membrane proteins, J. Mol. Biol. 229, 602-608.
    • (1993) J. Mol. Biol , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.F.4
  • 43
    • 0032717150 scopus 로고    scopus 로고
    • Design and characterization of anchoring amphiphilic peptides and their interactions with lipid vesicles
    • Percot, H., Zhu, X. X., and Lafleur, M. (1999) Design and characterization of anchoring amphiphilic peptides and their interactions with lipid vesicles, Biopolymers 50, 647-655.
    • (1999) Biopolymers , vol.50 , pp. 647-655
    • Percot, H.1    Zhu, X.X.2    Lafleur, M.3
  • 44
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. (1998) Hydrophobic mismatch between proteins and lipids in membranes, Biochim. Biophys. Acta 1376, 401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 45
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R. R., and Kilian, J. A. (2003) Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring, Mol. Membr. Biol. 20, 271-284.
    • (2003) Mol. Membr. Biol , vol.20 , pp. 271-284
    • de Planque, M.R.R.1    Kilian, J.A.2
  • 46
    • 0025882870 scopus 로고
    • Systematic analysis of stop-transfer sequence for microsomal membrane
    • Kuriowa, T., Sakaguchi, M., Mihara, K., and Omura, T. (1991) Systematic analysis of stop-transfer sequence for microsomal membrane, J. Biol. Chem. 266, 9251-9255.
    • (1991) J. Biol. Chem , vol.266 , pp. 9251-9255
    • Kuriowa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 47
    • 0029060799 scopus 로고
    • Artificial transmembrane segments. Requirement for stop transfer and polypeptide orientation
    • Chen, H., and Kendall, D. A. (1995) Artificial transmembrane segments. Requirement for stop transfer and polypeptide orientation, J. Biol. Chem. 270, 14115-14122.
    • (1995) J. Biol. Chem , vol.270 , pp. 14115-14122
    • Chen, H.1    Kendall, D.A.2
  • 49
    • 0028577485 scopus 로고
    • Semisynthetic proteins: Model systems for the study of the insertion of hydrophobic peptides into preformed lipid bilayers
    • Moll, T. S., and Thompson, T. E. (1994) Semisynthetic proteins: Model systems for the study of the insertion of hydrophobic peptides into preformed lipid bilayers, Biochemistry 33, 15469-15482.
    • (1994) Biochemistry , vol.33 , pp. 15469-15482
    • Moll, T.S.1    Thompson, T.E.2
  • 50
    • 0029757517 scopus 로고    scopus 로고
    • Design of membrane-inserting peptides: Spectroscopic characterization with and without lipid bilayers
    • Chung, L. A., and Thompson, T. E. (1996) Design of membrane-inserting peptides: Spectroscopic characterization with and without lipid bilayers, Biochemistry 35, 11343-11354.
    • (1996) Biochemistry , vol.35 , pp. 11343-11354
    • Chung, L.A.1    Thompson, T.E.2


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