메뉴 건너뛰기




Volumn 94, Issue 4, 2008, Pages 1315-1325

Influence of trifluoroethanol on membrane interfacial anchoring interactions of transmembrane α-helical peptides

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PEPTIDE; TRIFLUOROETHANOL; WATER;

EID: 38949198048     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.106.101782     Document Type: Article
Times cited : (21)

References (56)
  • 1
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. 2003. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta. 1612:1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 2
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
    • Dumas, F., M. C. Lebrun, and J. F. Tocanne. 1999. Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions? FEBS Lett. 458:271-277.
    • (1999) FEBS Lett , vol.458 , pp. 271-277
    • Dumas, F.1    Lebrun, M.C.2    Tocanne, J.F.3
  • 3
    • 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
  • 4
    • 20444366208 scopus 로고    scopus 로고
    • Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch
    • Park, S. H., and S. J. Opella. 2005. Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch. J. Mol. Biol. 350:310-318.
    • (2005) J. Mol. Biol , vol.350 , pp. 310-318
    • Park, S.H.1    Opella, S.J.2
  • 5
    • 33846562986 scopus 로고    scopus 로고
    • Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies
    • Ramamoorthy, A., S. K. Kandasamy, D.-K. Lee, S. Kidambi, and R. G. Larson. 2007. Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies. Biochemistry. 46:965-975.
    • (2007) Biochemistry , vol.46 , pp. 965-975
    • Ramamoorthy, A.1    Kandasamy, S.K.2    Lee, D.-K.3    Kidambi, S.4    Larson, R.G.5
  • 6
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. F. Reithmeier. 1993. Non-random distribution of amino acids 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
  • 7
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192.
    • (1994) Annu. Rev. Biophys. Biomol. Struct , vol.23 , pp. 167-192
    • von Heijne, G.1
  • 8
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • Reithmeier, R. A. F. 1995. Characterization and modeling of membrane proteins using sequence analysis. Curr. Opin. Struct. Biol. 5:491-500.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 491-500
    • Reithmeier, R.A.F.1
  • 9
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in trans-membrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque, M. R. R., B. B. Bonev, J. A. A. Demmers, D. V. Greathouse, R. E. Koeppe II, F. Separovic, A. Watts, and J. A. Killian. 2003. Interfacial anchor properties of tryptophan residues in trans-membrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry. 42:5341-5348.
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • de Planque, M.R.R.1    Bonev, B.B.2    Demmers, J.A.A.3    Greathouse, D.V.4    Koeppe II, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8
  • 10
    • 0035860765 scopus 로고    scopus 로고
    • Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spec- trometry
    • Demmers, J. A. A., E. Van Duijn, J. Haverkamp, D. V. Greathouse, R. E. I. I. Koeppe II, A. J. R. Heck, and J. A. Killian. 2001. Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spec- trometry. J. Biol. Chem. 276:34501-34508.
    • (2001) J. Biol. Chem , vol.276 , pp. 34501-34508
    • Demmers, J.A.A.1    Van Duijn, E.2    Haverkamp, J.3    Greathouse, D.V.4    Koeppe II, R.E.I.I.5    Heck, A.J.R.6    Killian, J.A.7
  • 11
    • 0001006658 scopus 로고
    • Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure
    • Davis, J. H., D. M. Clare, R. S. Hodges, and M. Bloom. 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
  • 12
    • 0032512417 scopus 로고    scopus 로고
    • Hydro-phobic mismatch and the incorporation of peptides into lipid bilayers: A possible mechanism for retention in the Golgi
    • Webb, R. J., J. M. East, R. P. Sharma, and A. G. Lee. 1998. Hydro-phobic mismatch and the incorporation of peptides into lipid bilayers: a possible mechanism for retention in the Golgi. Biochemistry. 37:673-679.
    • (1998) Biochemistry , vol.37 , pp. 673-679
    • Webb, R.J.1    East, J.M.2    Sharma, R.P.3    Lee, A.G.4
  • 13
    • 0033522486 scopus 로고    scopus 로고
    • Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length
    • Ren, J., S. Lew, J. Wang, and E. London. 1999. Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length. Biochemistry. 38:5905-5912.
    • (1999) Biochemistry , vol.38 , pp. 5905-5912
    • Ren, J.1    Lew, S.2    Wang, J.3    London, E.4
  • 15
    • 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 J. A. Killian. 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
  • 16
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic mem brane proteins
    • Killian, J. A. 2003. Synthetic peptides as models for intrinsic mem brane proteins. FEBS Lett. 555:134-138.
    • (2003) FEBS Lett , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 20
    • 2442716491 scopus 로고    scopus 로고
    • Small alcohols destabilize the KcsA tetramer via their effect on the membrane lateral pressure
    • van den Brink-van der Laan, E., V. Chupin, J. A. Killian, and B. De Kruijff. 2004. Small alcohols destabilize the KcsA tetramer via their effect on the membrane lateral pressure. Biochemistry. 43:5939-5942.
    • (2004) Biochemistry , vol.43 , pp. 5939-5942
    • van den Brink-van der Laan, E.1    Chupin, V.2    Killian, J.A.3    De Kruijff, B.4
  • 21
    • 23344450195 scopus 로고    scopus 로고
    • Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes
    • Spelbrink, R. E. J., A. Kolkman, M. Slijper, J. A. Killian, and B. De Kruijff. 2005. Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes. J. Biol. Chem. 280:28742-28748.
    • (2005) J. Biol. Chem , vol.280 , pp. 28742-28748
    • Spelbrink, R.E.J.1    Kolkman, A.2    Slijper, M.3    Killian, J.A.4    De Kruijff, B.5
  • 22
    • 0036198191 scopus 로고    scopus 로고
    • Nuclear overhauser enhancement spectroscopy cross-relaxation rates and ethanol distribution across membranes
    • Feller, S. E., C. A. Brown, D. T. Nizza, and K. Gawrisch. 2002. Nuclear overhauser enhancement spectroscopy cross-relaxation rates and ethanol distribution across membranes. Biophys. J. 82:1396-1404.
    • (2002) Biophys. J , vol.82 , pp. 1396-1404
    • Feller, S.E.1    Brown, C.A.2    Nizza, D.T.3    Gawrisch, K.4
  • 23
    • 0028352680 scopus 로고
    • Direct NMR evidence for ethanol binding to the lipid-water interface of phospholipid bilayers
    • Barry, J. A., and K. Gawrisch. 1994. Direct NMR evidence for ethanol binding to the lipid-water interface of phospholipid bilayers. Biochemistry. 33:8082-8088.
    • (1994) Biochemistry , vol.33 , pp. 8082-8088
    • Barry, J.A.1    Gawrisch, K.2
  • 24
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • Cantor,R.S. 1997. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. Biochemistry. 36:2339-2344.
    • (1997) Biochemistry , vol.36 , pp. 2339-2344
    • Cantor, R.S.1
  • 25
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of barrel-stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • Cantor, R. S. 2002. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys. J. 82:2520-2525.
    • (2002) Biophys. J , vol.82 , pp. 2520-2525
    • Cantor, R.S.1
  • 26
    • 17144372545 scopus 로고    scopus 로고
    • A convenient solid phase synthesis of S-palmitoyl transmembrane peptides
    • Rijkers, D. T. S., J. A. W. Kruijtzer, J. A. Killian, and R. M. J. Liskamp. 2005. A convenient solid phase synthesis of S-palmitoyl transmembrane peptides. Tetrahedron Lett. 46:3341-3345.
    • (2005) Tetrahedron Lett , vol.46 , pp. 3341-3345
    • Rijkers, D.T.S.1    Kruijtzer, J.A.W.2    Killian, J.A.3    Liskamp, R.M.J.4
  • 29
    • 0014779155 scopus 로고
    • Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., S. Fleisher, and A. Yamamoto. 1970. Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids. 5:494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleisher, S.2    Yamamoto, A.3
  • 34
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • Henzler-Wildman, K. A., G. V. Martinez, M. F. Brown, and A. Ramamoorthy. 2004. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry. 43:8459-8469.
    • (2004) Biochemistry , vol.43 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 37
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes. Biochim. Biophys. Acta. 515:105-140.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 39
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • de Planque, M. R. R., E. Goormaghtigh, D. V. Greathouse, R. E. Koeppe II, J. A. W. Kruijtzer, R. M. J. Liskamp, B. de Kruijff, and J. A. Killian. 2001. Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry. 40:5000-5010.
    • (2001) Biochemistry , vol.40 , pp. 5000-5010
    • de Planque, M.R.R.1    Goormaghtigh, E.2    Greathouse, D.V.3    Koeppe II, R.E.4    Kruijtzer, J.A.W.5    Liskamp, R.M.J.6    de Kruijff, B.7    Killian, J.A.8
  • 40
    • 0030888224 scopus 로고    scopus 로고
    • Determining ethanol distribution in phospholipid multilayers with MAS-NOESY spectra
    • Holte, L. L., and K. Gawrisch. 1997. Determining ethanol distribution in phospholipid multilayers with MAS-NOESY spectra. Biochemistry. 36:4669-4674.
    • (1997) Biochemistry , vol.36 , pp. 4669-4674
    • Holte, L.L.1    Gawrisch, K.2
  • 41
    • 0027982335 scopus 로고
    • Hydrogen bonding. 32. An analysis of water-octanol and water- alkane partitioning and the Δlog P parameter of Seiler
    • Abraham, M. H., H. S. Chadha, G. S. Whiting, and R. C. Mitchell. 1994. Hydrogen bonding. 32. An analysis of water-octanol and water- alkane partitioning and the Δlog P parameter of Seiler. J. Pharm. Sci. 83:1085-1100.
    • (1994) J. Pharm. Sci , vol.83 , pp. 1085-1100
    • Abraham, M.H.1    Chadha, H.S.2    Whiting, G.S.3    Mitchell, R.C.4
  • 42
    • 0040730144 scopus 로고
    • Dielectric constants of some organic solvent-water mixtures at various temperatures
    • Åkerlöf, G. 1932. Dielectric constants of some organic solvent-water mixtures at various temperatures. J. Am. Chem. Soc. 54:4125-4139.
    • (1932) J. Am. Chem. Soc , vol.54 , pp. 4125-4139
    • Åkerlöf, G.1
  • 43
    • 0033595582 scopus 로고    scopus 로고
    • Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides
    • Hong, D.-P., M. Hoshino, R. Kuboi, and Y. Goto. 1999. Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides. J. Am. Chem. Soc. 121:8427-8433.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 8427-8433
    • Hong, D.-P.1    Hoshino, M.2    Kuboi, R.3    Goto, Y.4
  • 44
    • 0001656775 scopus 로고
    • Physical properties and hydrogen-bonding in the system ethanol-2,2,2-trifluoro-ethanol
    • Mukherjee, L. M., and E. Grunwald. 1958. Physical properties and hydrogen-bonding in the system ethanol-2,2,2-trifluoro-ethanol. J. Phys. Chem. 62:1311-1314.
    • (1958) J. Phys. Chem , vol.62 , pp. 1311-1314
    • Mukherjee, L.M.1    Grunwald, E.2
  • 46
    • 0009999388 scopus 로고
    • Dielectric dispersion and relaxation mechanism in some trifluoro compounds at microwave frequencies
    • Purohith, H. D., H. S. Sharma, and A. D. Vyas. 1975. Dielectric dispersion and relaxation mechanism in some trifluoro compounds at microwave frequencies. Bull. Chem. Soc. Jpn. 48:327-329.
    • (1975) Bull. Chem. Soc. Jpn , vol.48 , pp. 327-329
    • Purohith, H.D.1    Sharma, H.S.2    Vyas, A.D.3
  • 47
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • Andersen, O. S., and R. E. Koeppe II. 2007. Bilayer thickness and membrane protein function: an energetic perspective. Annu. Rev. Biophys. Biomol. Struct. 36:107-130.
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 48
    • 33745634914 scopus 로고    scopus 로고
    • Regulation of membrane protein function by lipid bilayer elasticity-a single molecule technology to measure the bilayer properties experienced by an embedded protein
    • Lundbaek, J. A. 2006. Regulation of membrane protein function by lipid bilayer elasticity-a single molecule technology to measure the bilayer properties experienced by an embedded protein. J. Phys. Condens. Matter. 18:S1305-S1344.
    • (2006) J. Phys. Condens. Matter , vol.18
    • Lundbaek, J.A.1
  • 49
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • McIntosh, T. J., and S. A. Simon. 2006. Roles of bilayer material properties in function and distribution of membrane proteins. Annu. Rev. Biophys. Biomol. Struct. 35:177-198.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 50
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White, S. H., and W. C. Wimley. 1998. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta. 1376:339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 51
    • 0010243675 scopus 로고
    • Zur Theorie der Alkoholnarkose.
    • Meyer, H. H. 1899. Zur Theorie der Alkoholnarkose. Arch. Exp. Pathol. Pharmakol. 42:109-118.
    • (1899) Arch. Exp. Pathol. Pharmakol , vol.42 , pp. 109-118
    • Meyer, H.H.1
  • 53
    • 0021044761 scopus 로고
    • Membrane interactions with general and local anaesthetics: A review of molecular hypotheses of anaesthesia
    • Dluzewski, A. R., M. J. Halsey, and A. C. Simmonds. 1983. Membrane interactions with general and local anaesthetics: a review of molecular hypotheses of anaesthesia. Mol. Aspects Med. 6:461-573.
    • (1983) Mol. Aspects Med , vol.6 , pp. 461-573
    • Dluzewski, A.R.1    Halsey, M.J.2    Simmonds, A.C.3
  • 54
    • 0034023885 scopus 로고    scopus 로고
    • The actions of ether, alcohol and alkane general anaesthetics on GABAA and glycine receptors and the effects of TM2 and TM3 mutations
    • Krasowski, M. D., and N. L. Harrison. 2000. The actions of ether, alcohol and alkane general anaesthetics on GABAA and glycine receptors and the effects of TM2 and TM3 mutations. Br. J. Pharm. 129: 731-743.
    • (2000) Br. J. Pharm , vol.129 , pp. 731-743
    • Krasowski, M.D.1    Harrison, N.L.2
  • 55
    • 34249685982 scopus 로고    scopus 로고
    • An electrostatic/ hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins
    • Kooijman, E. E., D. P. Tieleman, C. Testerink, T. Munnik, D. T. Rijkers, K. N. Burger, and B. de Kruijff. 2007. An electrostatic/ hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins. J. Biol. Chem. 282:11356-11364.
    • (2007) J. Biol. Chem , vol.282 , pp. 11356-11364
    • Kooijman, E.E.1    Tieleman, D.P.2    Testerink, C.3    Munnik, T.4    Rijkers, D.T.5    Burger, K.N.6    de Kruijff, B.7
  • 56
    • 34147178808 scopus 로고    scopus 로고
    • 2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensi- tive channel MscS
    • Akitake, B., R. E. Spelbrink, A. Anishkin, J. A. Killian, B. de Kruijff, and S. Sukharev. 2007. 2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensi- tive channel MscS. Biophys. J. 92:2771-2784.
    • (2007) Biophys. J , vol.92 , pp. 2771-2784
    • Akitake, B.1    Spelbrink, R.E.2    Anishkin, A.3    Killian, J.A.4    de Kruijff, B.5    Sukharev, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.