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Volumn 26, Issue 5, 1997, Pages 405-416

A theoretical model for the association of amphiphilic transmembrane peptides in lipid bilayers

Author keywords

DPPC; Hydrophobic matching; Lipid peptide interaction; Monte Carlo simulation; Peptide aggregation

Indexed keywords

MEMBRANE PROTEIN;

EID: 0030839366     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050094     Document Type: Article
Times cited : (24)

References (56)
  • 2
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane α-helices of phospholamdan, a cardiac ion channel
    • Arkin IT, Adams PD, MacKenzie KR, Lemmon MA, Brünger AT, Engelman DM (1994) Structural organization of the pentameric transmembrane α-helices of phospholamdan, a cardiac ion channel. Embo J 13: 4757-4764
    • (1994) Embo J , vol.13 , pp. 4757-4764
    • Arkin, I.T.1    Adams, P.D.2    MacKenzie, K.R.3    Lemmon, M.A.4    Brünger, A.T.5    Engelman, D.M.6
  • 3
    • 0029768644 scopus 로고    scopus 로고
    • Helix-helix interactions in lipid bilayers
    • Ben-Tal N, Honig B (1996) Helix-helix interactions in lipid bilayers. Biophys J 71: 3046-3050
    • (1996) Biophys J , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2
  • 4
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann B-J, Knowles WJ, Marchesi VT (1989) Synthetic peptides mimic the assembly of transmembrane glycoproteins. J Biol Chem 264: 4033-4037
    • (1989) J Biol Chem , vol.264 , pp. 4033-4037
    • Bormann, B.-J.1    Knowles, W.J.2    Marchesi, V.T.3
  • 5
    • 0025936242 scopus 로고
    • Differentiation of lipid-associating helices by use of a three-dimensional molecular hydrophobicity potential calculations
    • Brasseur R (1991) Differentiation of lipid-associating helices by use of a three-dimensional molecular hydrophobicity potential calculations. J Biol Chem 266: 16 120-16 127
    • (1991) J Biol Chem , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 6
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia C (1976) The nature of the accessible and buried surfaces in proteins. J Mol Biol 105: 1-14
    • (1976) J Mol Biol , vol.105 , pp. 1-14
    • Chothia, C.1
  • 7
    • 0030034644 scopus 로고    scopus 로고
    • The G-protein nanomachine
    • Clapham D (1996) The G-protein nanomachine. Nature 379: 297-299
    • (1996) Nature , vol.379 , pp. 297-299
    • Clapham, D.1
  • 8
    • 0025819126 scopus 로고
    • Membrane protein association by potential intramembrane charge pairs
    • Cosson P, Lankford SP, Bonifacino JS, Klausner RD (1991) Membrane protein association by potential intramembrane charge pairs. Nature 351: 414-416
    • (1991) Nature , vol.351 , pp. 414-416
    • Cosson, P.1    Lankford, S.P.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 9
  • 10
    • 0024288356 scopus 로고
    • The structure of membrane-spanning polypeptide studied by molecular dynamics
    • Edholm O, Jähnig F (1988) The structure of membrane-spanning polypeptide studied by molecular dynamics. Biophys Chem 30: 279-292
    • (1988) Biophys Chem , vol.30 , pp. 279-292
    • Edholm, O.1    Jähnig, F.2
  • 12
    • 0022510143 scopus 로고
    • Identifying non polar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman DM, Steitz TA, Goldman A (1986) Identifying non polar transbilayer helices in amino acid sequences of membrane proteins. Ann Rev Biophys Biophys Chem 15: 321-353
    • (1986) Ann Rev Biophys Biophys Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 14
    • 0028178521 scopus 로고
    • Pore-forming peptides induce rapid phospholipid flip-flop in membranes
    • Fattal E, Nir S, Parente RA, Szoka FC Jr (1994) Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry 33: 6721-6731
    • (1994) Biochemistry , vol.33 , pp. 6721-6731
    • Fattal, E.1    Nir, S.2    Parente, R.A.3    Szoka F.C., Jr.4
  • 15
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit E, Boman A, Boman HG, Shai Y (1995) Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34: 11479-11488
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 16
    • 0029112313 scopus 로고
    • Forces and factors that contributed to the structural stability of membrane proteins
    • Haltia T, Freire E (1995) Forces and factors that contributed to the structural stability of membrane proteins. Biochim Biophys Acta 1241: 295-322
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 17
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He K, Ludke SJ, Huang HW, Worcester D (1995) Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 34: 15614-15618
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludke, S.J.2    Huang, H.W.3    Worcester, D.4
  • 18
    • 0030071247 scopus 로고    scopus 로고
    • A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering
    • Heimburg T, Biltonen RL (1996) A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering. Biophys J 70: 84-96
    • (1996) Biophys J , vol.70 , pp. 84-96
    • Heimburg, T.1    Biltonen, R.L.2
  • 19
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R, Unwin PNT (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257: 28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 20
    • 0000616967 scopus 로고
    • Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy
    • Huschilt JC, Hodges RS, Davis JH (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
  • 21
    • 0025269179 scopus 로고
    • Relationships between lipid membrane area, Hydrophobic thickness and acyl-chain orientational order. the effect of cholesterol
    • Ipsen JH, Mouritsen OG, Bloom M (1990 a) Relationships between lipid membrane area, Hydrophobic thickness and acyl-chain orientational order. The effect of cholesterol. Biophys J 57: 405-412
    • (1990) Biophys J , vol.57 , pp. 405-412
    • Ipsen, J.H.1    Mouritsen, O.G.2    Bloom, M.3
  • 22
    • 0025018331 scopus 로고
    • Density fluctuations in saturated phospholipid bilayers increase as the acyl-chain length decreases
    • Ipsen JH, Jørgensen K, Mouritsen OG (1990 b) Density fluctuations in saturated phospholipid bilayers increase as the acyl-chain length decreases. Biophys J 58: 1099-1107
    • (1990) Biophys J , vol.58 , pp. 1099-1107
    • Ipsen, J.H.1    Jørgensen, K.2    Mouritsen, O.G.3
  • 23
    • 0026642866 scopus 로고
    • Bacteriorphodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn TW, Engelman DM (1992) Bacteriorphodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 31: 6144-6151
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 24
    • 0029797094 scopus 로고    scopus 로고
    • Design and synthesis of amphiphilic α-helical peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- And bio-membranes
    • Kiyota T, Lee S, Sugihara G (1996) Design and synthesis of amphiphilic α-helical peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35: 13196-13204
    • (1996) Biochemistry , vol.35 , pp. 13196-13204
    • Kiyota, T.1    Lee, S.2    Sugihara, G.3
  • 26
    • 0025898707 scopus 로고
    • Three-dimensional structure of plant light-harvesting complex determined by electron crystallography
    • Külbrandt W, Wang DN (1991) Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 350: 130-134
    • (1991) Nature , vol.350 , pp. 130-134
    • Külbrandt, W.1    Wang, D.N.2
  • 27
    • 0000963997 scopus 로고
    • Helix-helix interactions inside lipid bilayers
    • Lemmon ME, Engelman DM (1992) Helix-helix interactions inside lipid bilayers. Curr Opin Struct Biol 2: 511-518
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 511-518
    • Lemmon, M.E.1    Engelman, D.M.2
  • 28
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon ME, Engelman DM (1994) Specificity and promiscuity in membrane helix interactions. Quat Rev Biophys 27: 157-218
    • (1994) Quat Rev Biophys , vol.27 , pp. 157-218
    • Lemmon, M.E.1    Engelman, D.M.2
  • 29
    • 0020491922 scopus 로고
    • Phase separation in lipid bilayers containing integral proteins. Computer simulation studies
    • Lookman T, Pink DA, Grundke EW, Zuckermann MJ, de Verteuil F (1982) Phase separation in lipid bilayers containing integral proteins. Computer simulation studies. Biochemistry 21: 5593-5601
    • (1982) Biochemistry , vol.21 , pp. 5593-5601
    • Lookman, T.1    Pink, D.A.2    Grundke, E.W.3    Zuckermann, M.J.4    De Verteuil, F.5
  • 30
    • 0029916523 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy and site-directed iso-tope labeling as a probe of local secondary structure in the transmembrane domain of phospholamdan
    • Ludlam CFC, Arkin IT, Liu X-M, Rothman MS, Rath P, Aimoto S, Smith SO, Engelman DM, Rothschild KJ (1996) Fourier transform infrared spectroscopy and site-directed iso-tope labeling as a probe of local secondary structure in the transmembrane domain of phospholamdan. Biophys J 70: 1728-1788
    • (1996) Biophys J , vol.70 , pp. 1728-1788
    • Ludlam, C.F.C.1    Arkin, I.T.2    Liu, X.-M.3    Rothman, M.S.4    Rath, P.5    Aimoto, S.6    Smith, S.O.7    Engelman, D.M.8    Rothschild, K.J.9
  • 31
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • Meyer E (1992) Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications. Protein Science 1: 1543-1562
    • (1992) Protein Science , vol.1 , pp. 1543-1562
    • Meyer, E.1
  • 32
    • 0022399766 scopus 로고
    • Simultaneous modelling of phase and calorimetric behavior in an amphiphilic peptide/ phospholipid model membrane
    • Morrow MR, Huschilt JC, Davis JH (1985) Simultaneous modelling 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
  • 35
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen OG, Bloom M (1984) Mattress model of lipid-protein interactions in membranes. Biophys J 46: 141-153
    • (1984) Biophys J , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 37
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thicknesses in model membranes
    • Nezil FA, Bloom M (1992) Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thicknesses in model membranes. Biophys J 61: 1176-1183
    • (1992) Biophys J , vol.61 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 38
    • 0021210050 scopus 로고
    • Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transition, and computer simulations of lipid-protein bilayers
    • Pink DA (1984) Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transition, and computer simulations of lipid-protein bilayers. Can J Biochem Cell Biol 62: 760-777
    • (1984) Can J Biochem Cell Biol , vol.62 , pp. 760-777
    • Pink, D.A.1
  • 39
    • 0019330568 scopus 로고
    • Raman scattering in bilayers of saturated phosphatidylcholines. Experiment and theory
    • Pink DA, Green JG, Chapman D (1980) Raman scattering in bilayers of saturated phosphatidylcholines. Experiment and theory. Biochemistry 19: 349-356
    • (1980) Biochemistry , vol.19 , pp. 349-356
    • Pink, D.A.1    Green, J.G.2    Chapman, D.3
  • 40
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α-helices are autonomous folding domain
    • Popot J-L (1993) Integral membrane protein structure: transmembrane α-helices are autonomous folding domain. Curr Opin Struct Biol 3: 532-540
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 532-540
    • Popot, J.-L.1
  • 41
    • 0025338423 scopus 로고
    • On the micro assembly of integral membrane proteins
    • Popot J-L, de Vitry C (1990) On the micro assembly of integral membrane proteins. Ann Rev Biophys Biophys Chem 19: 369-403
    • (1990) Ann Rev Biophys Biophys Chem , vol.19 , pp. 369-403
    • Popot, J.-L.1    De Vitry, C.2
  • 42
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J-L, Engelman DM (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29: 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 43
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees DC, DeAntonio L, Eisenberg D (1989) Hydrophobic organization of membrane proteins. Science 245: 510-512
    • (1989) Science , vol.245 , pp. 510-512
    • Rees, D.C.1    DeAntonio, L.2    Eisenberg, D.3
  • 44
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai Y (1995) Molecular recognition between membrane-spanning polypeptides. Trends Biochem Science 20: 460-464
    • (1995) Trends Biochem Science , vol.20 , pp. 460-464
    • Shai, Y.1
  • 46
    • 0024400738 scopus 로고
    • Theory of protein-induced lateral phase separation in lipid membranes
    • Sperotto MM, Ipsen JH, Mouritsen OG (1989) Theory of protein-induced lateral phase separation in lipid membranes. Cell Biophysics 14: 79-95
    • (1989) Cell Biophysics , vol.14 , pp. 79-95
    • Sperotto, M.M.1    Ipsen, J.H.2    Mouritsen, O.G.3
  • 47
    • 0001768252 scopus 로고
    • Dependence of lipid membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness
    • Sperotto MM, Mouritsen OG (1988) Dependence of lipid membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness. Eur Biophys J 16: 1-10
    • (1988) Eur Biophys J , vol.16 , pp. 1-10
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 48
    • 0025971506 scopus 로고
    • Mean-field and Monte Carlo simulation studies of the lateral distribution of proteins in membranes
    • Sperotto MM, Mouritsen OG (1991) Mean-field and Monte Carlo simulation studies of the lateral distribution of proteins in membranes. Eur Biophys J 19: 157-168
    • (1991) Eur Biophys J , vol.19 , pp. 157-168
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 52
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G, Gavel Y (1988) Topogenic signals in integral membrane proteins. Eur J Biochem 174: 671-678
    • (1988) Eur J Biochem , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 53
    • 0025681503 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne G, Manoil M (1990) Membrane proteins: from sequence to structure. Protein Engineering 4: 109-112
    • (1990) Protein Engineering , vol.4 , pp. 109-112
    • Von Heijne, G.1    Manoil, M.2
  • 54
    • 0025989688 scopus 로고
    • Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase?
    • Wang J, Pullman A (1991) Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase? Biochim Biophys Acta 1070: 493-496
    • (1991) Biochim Biophys Acta , vol.1070 , pp. 493-496
    • Wang, J.1    Pullman, A.2
  • 55
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetry and FTIR spectroscopic studies
    • Zhang Y-P, Lewis RNAH, Hodges RS, McElhaney RN (1992) Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetry 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


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