메뉴 건너뛰기




Volumn 39, Issue 3, 2006, Pages 176-183

Solid-state NMR studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BIOPOLYMER; MEMBRANE PROTEIN; PEPTIDE;

EID: 33645505791     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar040037e     Document Type: Review
Times cited : (45)

References (49)
  • 1
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E.; Lehrer, R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998, 16, 82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 4
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1998, 1376, 391-400.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 5
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1999, 1462, 157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 6
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M.; Vogel, H. J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462, 11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 8
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang, Y. Q.; Yuan, J.; Osapay, G.; Osapay, K.; Tran, D.; Miller, C. J.; Ouellette, A. J.; Selsted, M. E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 1999, 286, 498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 11
    • 84886025282 scopus 로고    scopus 로고
    • Ramamoorthy, A., Ed.; CRC Press Taylor and Francis Group: Boca Raton, FL
    • Hong, M.; Wi, S. In NMR Spectroscopy of Biological Solids; Ramamoorthy, A., Ed.; CRC Press Taylor and Francis Group: Boca Raton, FL, 2006; pp 87-122.
    • (2006) NMR Spectroscopy of Biological Solids , pp. 87-122
    • Hong, M.1    Wi, S.2
  • 13
    • 0034685511 scopus 로고    scopus 로고
    • 13Cα Chemical Shift Anisotropies for the Identification of Protein Secondary Structure
    • 13Cα Chemical Shift Anisotropies for the Identification of Protein Secondary Structure. J. Am. Chem. Soc. 2000, 122, 3762-3770.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3762-3770
    • Hong, M.1
  • 14
    • 0037066607 scopus 로고    scopus 로고
    • Conformational changes of colicin Ia channel-forming domain upon membrane binding: A solid-state NMR study
    • Huster, D.; Yao, X.; Jakes, K.; Hong, M. Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study. Biochim. Biophys. Acta 2002, 1561, 159-170.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 159-170
    • Huster, D.1    Yao, X.2    Jakes, K.3    Hong, M.4
  • 15
    • 0034703698 scopus 로고    scopus 로고
    • Efficient β-sheet Identification in Proteins by Solid-State NMR Spectroscopy
    • Huster, D.; Yamaguchi, S.; Hong, M. Efficient β-sheet Identification in Proteins by Solid-State NMR Spectroscopy. J. Am. Chem. Soc. 2000, 122, 11320-11327.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11320-11327
    • Huster, D.1    Yamaguchi, S.2    Hong, M.3
  • 16
    • 0031189051 scopus 로고    scopus 로고
    • Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR
    • Hong, M.; Gross, J. D.; Griffin, R. G. Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR. J. Phys. Chem. B 1997, 101, 5869-5874.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5869-5874
    • Hong, M.1    Gross, J.D.2    Griffin, R.G.3
  • 17
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR Spectroscopy
    • Opella, S. J.; Marassi, F. M. Structure determination of membrane proteins by NMR Spectroscopy. Chem. Rev. 2004, 104, 3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 18
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi, F. M.; Opella, S. J. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson. 2000, 144, 150-155.
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 20
    • 0037031254 scopus 로고    scopus 로고
    • Solid-State NMR Investigations of Peptide-Lipid Interaction and Orientation of a β-Sheet Antimicrobial Peptide, Protegrin
    • Yamaguchi, S.; Waring, A.; Hong, T.; Lehrer, R.; Hong, M. Solid-State NMR Investigations of Peptide-Lipid Interaction and Orientation of a β-Sheet Antimicrobial Peptide, Protegrin. Biochemistry 2002, 41, 9852-9862.
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Waring, A.2    Hong, T.3    Lehrer, R.4    Hong, M.5
  • 22
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. Action of antimicrobial peptides: two-state model. Biochemistry 2000, 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 25
    • 0026729232 scopus 로고
    • Structure of a fluid DOPC bilayer determined by joint refinement of X-ray and neutron diffraction data III Complete structure
    • Wiener, M. C.; White, S. H. Structure of a fluid DOPC bilayer determined by joint refinement of X-ray and neutron diffraction data III Complete structure. Biophys. J. 1992, 61, 434-447.
    • (1992) Biophys. J. , vol.61 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 26
    • 0032572058 scopus 로고    scopus 로고
    • A novel tool for probing membrane protein structure: Solid-state NMR with proton spin diffusion and X-nucleus detection
    • Kumashiro, K. K.; Schmidt-Rohr, K.; Murphy, O. J.; Ouellette, K. L.; Cramer, W. A.; Thompson, L. K. A novel tool for probing membrane protein structure: solid-state NMR with proton spin diffusion and X-nucleus detection. J. Am. Chem. Soc. 1998, 120, 5043-5051.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5043-5051
    • Kumashiro, K.K.1    Schmidt-Rohr, K.2    Murphy, O.J.3    Ouellette, K.L.4    Cramer, W.A.5    Thompson, L.K.6
  • 27
    • 2942704069 scopus 로고    scopus 로고
    • Solid-state NMR spin diffusion for measurement of membrane-bound peptide structure: Gramicidin A
    • Gallagher, G. J.; Hong, M.; Thompson, L. K. Solid-state NMR spin diffusion for measurement of membrane-bound peptide structure: gramicidin A. Biochemistry 2004, 43, 7899-7906.
    • (2004) Biochemistry , vol.43 , pp. 7899-7906
    • Gallagher, G.J.1    Hong, M.2    Thompson, L.K.3
  • 28
    • 0037028547 scopus 로고    scopus 로고
    • 1H Spin Diffusion from Lipids Using Solid-State NMR Spectroscopy
    • 1H Spin Diffusion from Lipids Using Solid-State NMR Spectroscopy. J. Am. Chem. Soc. 2002, 124, 874-883.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 874-883
    • Huster, D.1    Yao, X.L.2    Hong, M.3
  • 29
    • 0024961641 scopus 로고
    • Structure of the membrane-pore-forming fragment of colicin A
    • Parker, M. W.; Pattus, F.; Tucker, A. D.; Tsernoglou, D. Structure of the membrane-pore-forming fragment of colicin A. Nature 1989, 337, 93-96.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsernoglou, D.4
  • 30
    • 0031036238 scopus 로고    scopus 로고
    • Structure of DNA-cationic liposome complexes: DNA intercalation in multi-lamellar membranes in distinct interhelical packing regimes
    • Radler, J. O.; Koltover, I.; Salditt, T.; Safinya, C. R. Structure of DNA-cationic liposome complexes: DNA intercalation in multi-lamellar membranes in distinct interhelical packing regimes. Science 1997, 275, 810-814.
    • (1997) Science , vol.275 , pp. 810-814
    • Radler, J.O.1    Koltover, I.2    Salditt, T.3    Safinya, C.R.4
  • 31
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L.; Engelman, D. M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990, 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 32
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homooligomeric helical bundles
    • DeGrado, W. F.; Gratkowski, H.; Lear, J. D. How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homooligomeric helical bundles. Protein Sci. 2003, 12, 647-665.
    • (2003) Protein Sci. , vol.12 , pp. 647-665
    • DeGrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 34
    • 16244391442 scopus 로고    scopus 로고
    • Determination of Peptide Oligomerization in Lipid Membranes with Magic-Angle Spinning Spin Diffusion NMR
    • Buffy, J. J.; Waring, A. J.; Hong, M. Determination of Peptide Oligomerization in Lipid Membranes with Magic-Angle Spinning Spin Diffusion NMR. J. Am. Chem. Soc. 2005, 127, 4477-4483.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4477-4483
    • Buffy, J.J.1    Waring, A.J.2    Hong, M.3
  • 35
    • 0033568053 scopus 로고    scopus 로고
    • Centerband-only detection of exchange: Efficient analysis of dynamics in solids by NMR
    • deAzevedo, E. R.; Bonagamba, T. J.; Hu, W.; Schmidt-Rohr, K. Centerband-only detection of exchange: efficient analysis of dynamics in solids by NMR. J. Am. Chem. Soc. 1999, 121, 8411-8412.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8411-8412
    • DeAzevedo, E.R.1    Bonagamba, T.J.2    Hu, W.3    Schmidt-Rohr, K.4
  • 37
    • 26444593282 scopus 로고    scopus 로고
    • Intermolecular Packing and Alignment in an Ordered β-Hairpin Antimicrobial Peptide Aggregate from 2D Solid-State NMR
    • Tang, M.; Waring, A. J.; Hong, M. Intermolecular Packing and Alignment in an Ordered β-Hairpin Antimicrobial Peptide Aggregate from 2D Solid-State NMR. J. Am. Chem. Soc. 2005, 127, 13919-13927.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13919-13927
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 38
    • 0019960215 scopus 로고
    • Protein dynamics and NMR relaxation: Comparison of simulations with experiment
    • Lipari, G.; Szabo, A.; Levy, R. M. Protein dynamics and NMR relaxation: comparison of simulations with experiment. Nature 1982, 300, 197-198.
    • (1982) Nature , vol.300 , pp. 197-198
    • Lipari, G.1    Szabo, A.2    Levy, R.M.3
  • 39
    • 0037173873 scopus 로고    scopus 로고
    • Investigation of molecular motions by Lee-Goldburg cross-polarization NMR spectroscopy
    • Hong, M.; Yao, X. L.; Jakes, K.; Huster, D. Investigation of molecular motions by Lee-Goldburg cross-polarization NMR spectroscopy. J. Phys. Chem. B 2002, 106, 7355-7364.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7355-7364
    • Hong, M.1    Yao, X.L.2    Jakes, K.3    Huster, D.4
  • 40
    • 0035954376 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the dynamics of colicin Ia channel-forming domain
    • Huster, D.; Xiao, L. S.; Hong, M. Solid-State NMR Investigation of the dynamics of colicin Ia channel-forming domain. Biochemistry 2001, 40, 7662-7674.
    • (2001) Biochemistry , vol.40 , pp. 7662-7674
    • Huster, D.1    Xiao, L.S.2    Hong, M.3
  • 41
    • 30144444605 scopus 로고    scopus 로고
    • Effects of Anionic Lipid and Ion Concentrations on the Topology and Segmental Mobility of Colicin Ia Channel Domain from Solid-State NMR
    • Yao, X. L.; Hong, M. Effects of Anionic Lipid and Ion Concentrations on the Topology and Segmental Mobility of Colicin Ia Channel Domain from Solid-State NMR. Biochemistry 2006, 45, 289-295.
    • (2006) Biochemistry , vol.45 , pp. 289-295
    • Yao, X.L.1    Hong, M.2
  • 42
    • 0345276804 scopus 로고    scopus 로고
    • Immobilization and Aggregation of Antimicrobial Peptide Protegrin in Lipid Bilayers Investigated by Solid-State NMR
    • Buffy, J. J.; Waring, A. J.; Lehrer, R. I.; Hong, M. Immobilization and Aggregation of Antimicrobial Peptide Protegrin in Lipid Bilayers Investigated by Solid-State NMR. Biochemistry 2003, 42, 13725-13734.
    • (2003) Biochemistry , vol.42 , pp. 13725-13734
    • Buffy, J.J.1    Waring, A.J.2    Lehrer, R.I.3    Hong, M.4
  • 43
    • 0001123769 scopus 로고
    • High-resolution NMR spectra of orientated molecules
    • Saupe, A.; Englert, G. High-resolution NMR spectra of orientated molecules. Phys. Rev. Lett. 1963, 11, 462-464.
    • (1963) Phys. Rev. Lett. , vol.11 , pp. 462-464
    • Saupe, A.1    Englert, G.2
  • 44
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by Solid-State NMR
    • Yamaguchi, S.; Huster, D.; Waring, A.; Lehrer, R. I.; Tack, B. F.; Kearney, W.; Hong, M. Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by Solid-State NMR. Biophys. J. 2001, 81, 2203-2214.
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Tack, B.F.5    Kearney, W.6    Hong, M.7
  • 47
    • 7244257317 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the Selective Disruption of Lipid Membranes by Protegrin-1
    • Mani, R.; Buffy, J. J.; Waring, A. J.; Lehrer, R. I.; Hong, M. Solid-State NMR Investigation of the Selective Disruption of Lipid Membranes by Protegrin-1. Biochemistry 2004, 43, 13839-13848.
    • (2004) Biochemistry , vol.43 , pp. 13839-13848
    • Mani, R.1    Buffy, J.J.2    Waring, A.J.3    Lehrer, R.I.4    Hong, M.5
  • 48
    • 3342900055 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the Selective Perturbation of Lipid Bilayers by the Cyclic Antimicrobial Peptide RTD-1
    • Buffy, J. J.; McCormick, M. J.; Wi, S.; Waring, A.; Lehrer, R. I.; Hong, M. Solid-State NMR Investigation of the Selective Perturbation of Lipid Bilayers by the Cyclic Antimicrobial Peptide RTD-1. Biochemistry 2004, 43, 9800-9812.
    • (2004) Biochemistry , vol.43 , pp. 9800-9812
    • Buffy, J.J.1    McCormick, M.J.2    Wi, S.3    Waring, A.4    Lehrer, R.I.5    Hong, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.