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Volumn 90, Issue 5, 2006, Pages 1676-1686

Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: Structural fidelity of 2H-labels versus high sensitivity of 19F-NMR

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; PHENYLGLYCINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN PGLA; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; DEUTERIUM; FLUORINE; MEMBRANE PROTEIN; PEPTIDE GLY LEU AMIDE; PEPTIDE-GLY-LEU-AMIDE;

EID: 33646135796     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.073858     Document Type: Article
Times cited : (106)

References (51)
  • 1
    • 17844376024 scopus 로고    scopus 로고
    • NMR methods for studying membrane-active antimicrobial peptides
    • Strandberg, E., and A. S. Ulrich. 2004. NMR methods for studying membrane-active antimicrobial peptides. Concept. Magnetic. Res. A. 23A:89-120.
    • (2004) Concept. Magnetic. Res. A , vol.23 A , pp. 89-120
    • Strandberg, E.1    Ulrich, A.S.2
  • 2
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., and F. M. Marassi. 2004. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104:3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 6
    • 0002557818 scopus 로고    scopus 로고
    • 19F solid state NMR
    • J. Lindon, G. Tranter, and J. Holmes, editors. Academic Press, London
    • 19F solid state NMR. In Encyclopedia of Spectroscopy and Spectrometry. J. Lindon, G. Tranter, and J. Holmes, editors. Academic Press, London. 813-825.
    • (2000) Encyclopedia of Spectroscopy and Spectrometry , pp. 813-825
    • Ulrich, A.S.1
  • 9
    • 0042536464 scopus 로고    scopus 로고
    • Susceptibility corrections in solid-state NMR experiments with oriented membrane samples. Part I: Applications
    • Glaser, R. W., and A. S. Ulrich. 2003. Susceptibility corrections in solid-state NMR experiments with oriented membrane samples. Part I: applications. J. Magn. Reson. 164:104-114.
    • (2003) J. Magn. Reson. , vol.164 , pp. 104-114
    • Glaser, R.W.1    Ulrich, A.S.2
  • 12
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes. Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal, G., and R. Nagaraj. 1994. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes. Facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta. 1197:109-131.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 13
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M., and H. J. Vogel. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta. 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 16
    • 0020985676 scopus 로고
    • A novel peptide designated PYLa and its precursor as predicted from cloned mRNA of Xenopus laevis skin
    • Hoffmann, W., K. Richter, and G. Kreil. 1983. A novel peptide designated PYLa and its precursor as predicted from cloned mRNA of Xenopus laevis skin. EMBO J. 2:711-714 .
    • (1983) EMBO J. , vol.2 , pp. 711-714
    • Hoffmann, W.1    Richter, K.2    Kreil, G.3
  • 17
    • 0024286949 scopus 로고
    • Antimicrobial properties of peptides from Xenopus granular gland secretions
    • Soravia, E., G. Martini, and M. Zasloff. 1988. Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228:337-340.
    • (1988) FEBS Lett. , vol.228 , pp. 337-340
    • Soravia, E.1    Martini, G.2    Zasloff, M.3
  • 18
    • 0022373231 scopus 로고
    • Biosynthesis of peptides in the skin of Xenopus laevis: Isolation of novel peptides predicted from the sequence of cloned cDNAs
    • Richter, K., H. Aschauer, and G. Kreil. 1985. Biosynthesis of peptides in the skin of Xenopus laevis: isolation of novel peptides predicted from the sequence of cloned cDNAs. Peptides. 6(Suppl. 3):17-21.
    • (1985) Peptides , vol.6 , Issue.3 SUPPL. , pp. 17-21
    • Richter, K.1    Aschauer, H.2    Kreil, G.3
  • 19
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. 1987. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA. 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 20
    • 0031903306 scopus 로고    scopus 로고
    • Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., M. Zasloff, and S. J. Opella. 1998. Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy. Biophys. J. 74:981-987.
    • (1998) Biophys. J. , vol.74 , pp. 981-987
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 22
    • 0036343921 scopus 로고    scopus 로고
    • Dimer structure of magainin 2 bound to phospholipid vesicles
    • Wakamatsu, K., A. Takeda, T. Tachi, and K. Matsuzaki. 2002. Dimer structure of magainin 2 bound to phospholipid vesicles. Biopolymers. 64:314-327.
    • (2002) Biopolymers , vol.64 , pp. 314-327
    • Wakamatsu, K.1    Takeda, A.2    Tachi, T.3    Matsuzaki, K.4
  • 24
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. 1998. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta. 1376:391-400.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 25
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. 1999. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta. 1462:55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 26
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. 2000. Action of antimicrobial peptides: two-state model. Biochemistry. 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 27
    • 0032546613 scopus 로고    scopus 로고
    • 2H NMR study of peptide phosphorylation effects in a bilayer environment
    • 2H NMR study of peptide phosphorylation effects in a bilayer environment. Biochemistry. 37:7504-7508.
    • (1998) Biochemistry , vol.37 , pp. 7504-7508
    • Jones, D.H.1    Barber, K.R.2    Grant, C.W.M.3
  • 29
    • 0036434495 scopus 로고    scopus 로고
    • Methods for studying transmembrane peptides in bicelles: Consequences of hydrophobic mismatch and peptide sequence
    • Whiles, J. A., K. J. Glover, R. R. Vold, and E. A. Komives. 2002. Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence. J. Magn. Reson. 158:149-156.
    • (2002) J. Magn. Reson. , vol.158 , pp. 149-156
    • Whiles, J.A.1    Glover, K.J.2    Vold, R.R.3    Komives, E.A.4
  • 30
    • 0842286074 scopus 로고    scopus 로고
    • Structure determination of aligned samples of membrane proteins by NMR spectroscopy
    • Nevzorov, A. A., M. F. Mesleh, and S. J. Opella. 2004. Structure determination of aligned samples of membrane proteins by NMR spectroscopy. Magn. Reson. Chem. 42:162-171.
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 162-171
    • Nevzorov, A.A.1    Mesleh, M.F.2    Opella, S.J.3
  • 31
    • 33947091567 scopus 로고
    • 9-Fluorenylmethoxycarbonyl amino protecting group
    • Carpino, L. A., and G. Y. Han. 1972. 9-Fluorenylmethoxycarbonyl amino protecting group. J. Org. Chem. 37:3404-3409.
    • (1972) J. Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 32
    • 0025232814 scopus 로고
    • Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B., and R. L. Noble. 1990. Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35:161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 33
    • 2442767079 scopus 로고
    • Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media - Phase-cycled Hahn echo spectroscopy
    • Rance, M., and R. A. Byrd. 1983. Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media - phase-cycled Hahn echo spectroscopy. J. Magn. Reson. 52:221-240.
    • (1983) J. Magn. Reson. , vol.52 , pp. 221-240
    • Rance, M.1    Byrd, R.A.2
  • 35
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., K. R. Jeffrey, M. Bloom, M. I. Valic, and T. P. Higgs. 1976. Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42:390-394.
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 38
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin
    • Yamaguchi, S., T. Hong, A. Waring, R. I. Lehrer, and M. Hong. 2002. Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin. Biochemistry. 41:9852-9862.
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 40
    • 0026447195 scopus 로고
    • Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR
    • Ulrich, A. S., M. P. Heyn, and A. Watts. 1992. Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR. Biochemistry. 31:10390-10399.
    • (1992) Biochemistry , vol.31 , pp. 10390-10399
    • Ulrich, A.S.1    Heyn, M.P.2    Watts, A.3
  • 41
    • 0027588286 scopus 로고
    • 2H-NMR lineshapes of immobilized uniaxially oriented membrane proteins
    • 2H-NMR lineshapes of immobilized uniaxially oriented membrane proteins. Solid State Nucl. Magn. Reson. 2:21-36.
    • (1993) Solid State Nucl. Magn. Reson. , vol.2 , pp. 21-36
    • Ulrich, A.S.1    Watts, A.2
  • 43
    • 0029270249 scopus 로고
    • Re-alignment of the retinal chromophore in the M-photointermediate of bacteriorhodopsin
    • Ulrich, A. S., I. Wallat, M. P. Heyn, and A. Watts. 1995. Re-alignment of the retinal chromophore in the M-photointermediate of bacteriorhodopsin. Nat. Struct. Biol. 2:190-192.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 190-192
    • Ulrich, A.S.1    Wallat, I.2    Heyn, M.P.3    Watts, A.4
  • 45
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects
    • Wieprecht, T., O. Apostolov, M. Beyermann, and J. Seelig. 2000. Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects. Biochemistry. 39:442-452.
    • (2000) Biochemistry , vol.39 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 47
    • 0001675109 scopus 로고
    • Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides
    • Zhou, N. E., B. Y. Zhu, B. D. Sykes, and R. S. Hodges. 1992. Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides. J. Am. Chem. Soc. 114:4320-4326.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4320-4326
    • Zhou, N.E.1    Zhu, B.Y.2    Sykes, B.D.3    Hodges, R.S.4
  • 48
    • 0026029051 scopus 로고
    • Amide chemical shifts in many helices in peptides and proteins are periodic
    • Kuntz, I. D., P. A. Kosen, and E. C. Craig. 1991. Amide chemical shifts in many helices in peptides and proteins are periodic. J. Am. Chem. Soc. 113:1406-1408.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1406-1408
    • Kuntz, I.D.1    Kosen, P.A.2    Craig, E.C.3
  • 49
    • 3042736841 scopus 로고    scopus 로고
    • Secondary structure and lipid contact of a peptide antibiotic in phospholipid bilayers by REDOR
    • Toke, O., W. L. Maloy, S. J. Kim, J. Blazyk, and J. Schaefer. 2004. Secondary structure and lipid contact of a peptide antibiotic in phospholipid bilayers by REDOR. Biophys. J. 87:662-674.
    • (2004) Biophys. J. , vol.87 , pp. 662-674
    • Toke, O.1    Maloy, W.L.2    Kim, S.J.3    Blazyk, J.4    Schaefer, J.5
  • 50
    • 0034268554 scopus 로고    scopus 로고
    • 19F dipolar couplings within a trifluoromethyl-group are revealed by multipulse solid state NMR
    • 19F dipolar couplings within a trifluoromethyl-group are revealed by multipulse solid state NMR. J. Magn. Reson. 146:81-88.
    • (2000) J. Magn. Reson. , vol.146 , pp. 81-88
    • Grage, S.L.1    Ulrich, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.