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Volumn 43, Issue 30, 2004, Pages 9800-9812

Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; BACTERIA; BINDING ENERGY; BIOLOGICAL MATERIALS; CHOLESTEROL; COMPOSITION; LIPIDS; NUCLEAR MAGNETIC RESONANCE;

EID: 3342900055     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036243w     Document Type: Article
Times cited : (58)

References (64)
  • 2
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura, T., Furunaka, H., Miyata, T., Tokunaga, F., Muta, T., Iwanaga, S., Niwa, M., Takao, T., and Shimonishi, Y. (1988) Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure, J. Biol. Chem. 263, 16709-16713.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 3
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides at mammulian cells
    • Lehrer, R. I., Lichtenstein, A. K., and Ganz, T. (1993) Defensins: antimicrobial and cytotoxic peptides at mammulian cells, Annu. Rev. Immunol. 11, 105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 5
    • 0034488452 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides and their multifunctional role in the immune system
    • Scott, M. G., and Hancock, R. E. (2000) Cationic antimicrobial peptides and their multifunctional role in the immune system, Crit. Rev. Immunol. 20, 407-431.
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 407-431
    • Scott, M.G.1    Hancock, R.E.2
  • 6
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E., and Lehrer, R. (1998) Cationic peptides: a new source of antibiotics, Trends Biotechnol. 16, 82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 7
    • 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
  • 8
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin
    • Yamaguchi, S., Hong, T., Waring, A., Lehrer, R. I., and Hong, M. (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
  • 10
    • 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., and Hong, M. (2003) Immobilization and Aggregation of Antimicrobial Peptide Protegrin in Lipid Bilayers Investigated by Solid-State NMR, Biochemistry 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
  • 11
    • 0037108278 scopus 로고    scopus 로고
    • Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives
    • Laederach, A., Andreotti, A. H., and Fulton, D. B. (2002) Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives, Biochemistry 41, 12359-12368.
    • (2002) Biochemistry , vol.41 , pp. 12359-12368
    • Laederach, A.1    Andreotti, A.H.2    Fulton, D.B.3
  • 12
    • 0037031240 scopus 로고    scopus 로고
    • Two states of cyclic antimicrobial peptide RTD-1 in lipid bilayers
    • Weiss, T. M., Yang, L., Ding, L., Waring, A. J., Lehrer, R. I., and Huang, H. W. (2002) Two states of cyclic antimicrobial peptide RTD-1 in lipid bilayers, Biochemistry 41, 10070-10076.
    • (2002) Biochemistry , vol.41 , pp. 10070-10076
    • Weiss, T.M.1    Yang, L.2    Ding, L.3    Waring, A.J.4    Lehrer, R.I.5    Huang, H.W.6
  • 13
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. (1999) The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy, Biochim. Biophys. Acta 1462, 157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 14
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., Rapaport, D., Mor, A., Nicolas, P., and Shai, Y. (1992) Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes, Biochemistry 31, 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 15
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., Zasloff, M., and Opella, S. J. (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy, Protein Sci. 2, 2077-2084.
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 16
    • 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., Zasloff, M., and Opella, S. J. (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
  • 17
    • 0032763732 scopus 로고    scopus 로고
    • Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy
    • Marassi, F. M., Opella, S. J., Juvvadi, P., and Merrifield, R. B. (1999) Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy, Biophys. J. 77, 3152-3155.
    • (1999) Biophys. J. , vol.77 , pp. 3152-3155
    • Marassi, F.M.1    Opella, S.J.2    Juvvadi, P.3    Merrifield, R.B.4
  • 18
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He, K., Ludtke, S. J., Huang, H. W., and Worcester, D. L. (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    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4
  • 19
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He, K., Ludtke, S. J., Heller, W. T., and Huang, H. W. (1996) Mechanism of alamethicin insertion into lipid bilayers, Biophys. J. 71, 2669-2679.
    • (1996) Biophys. J. , vol.71 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 21
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • Yang, L., Weiss, T. M., Lehrer, R. I., and Huang, H. W. (2000) Crystallization of antimicrobial pores in membranes: magainin and protegrin, Biophys. J. 79, 2002-2009.
    • (2000) Biophys. J. , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 22
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock, K. J., Lee, D. K., and Ramamoorthy, A. (2003) MSI-78, an Analogue of the Magainin Antimicrobial Peptides, Disrupts Lipid Bilayer Structure via Positive Curvature Strain, Biophys. J. 84, 3052-3060.
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 23
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins
    • Tang, Y. Q., Yuan, J., Osapay, G., Osapay, K., Tran, D., Miller, C. J., Ouellette, A. J., and Selsted, M. E. (1999) A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins, Science 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
  • 24
    • 0036479317 scopus 로고    scopus 로고
    • Homodimeric θ-defensins from rhesus macaque leukocytes: Isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides
    • Tran, D., Tran, P. A., Tang, Y. Q., Yuan, J., Cole, T., and Selsted, M. E. (2002) Homodimeric θ-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides, J. Biol. Chem. 277, 3079-3084.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3079-3084
    • Tran, D.1    Tran, P.A.2    Tang, Y.Q.3    Yuan, J.4    Cole, T.5    Selsted, M.E.6
  • 25
    • 0035836463 scopus 로고    scopus 로고
    • Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from rhesus macaque leukocytes
    • Trabi, M., Schirra, H. J., and Craik, D. J. (2001) Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from rhesus macaque leukocytes, Biochemistry 40, 4211-4221.
    • (2001) Biochemistry , vol.40 , pp. 4211-4221
    • Trabi, M.1    Schirra, H.J.2    Craik, D.J.3
  • 26
    • 0034719492 scopus 로고    scopus 로고
    • Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-β-strand cystine knot framework
    • Tam, J. P., Lu, Y. A., and Yang, J. L. (2000) Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-β-strand cystine knot framework, Biochem. Biophys. Res. Commun. 267, 783-790.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 783-790
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 27
    • 0034113230 scopus 로고    scopus 로고
    • Membranolytic selectivity of cystine-stabilized cyclic protegrins
    • Tam, J. P., Wu, C., and Yang, J. L. (2000) Membranolytic selectivity of cystine-stabilized cyclic protegrins, Eur. J. Biochem. 267, 3289-3300.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3289-3300
    • Tam, J.P.1    Wu, C.2    Yang, J.L.3
  • 28
    • 0006627015 scopus 로고    scopus 로고
    • Static and magic angle spinning NMR of membrane peptides and proteins
    • Davis, J. H., and Auger, M. (1999) Static and magic angle spinning NMR of membrane peptides and proteins, Prog. NMR Spectrosc. 35, 1-84.
    • (1999) Prog. NMR Spectrosc. , vol.35 , pp. 1-84
    • Davis, J.H.1    Auger, M.2
  • 29
    • 0031764019 scopus 로고    scopus 로고
    • NMR structural studies of membrane proteins
    • Marassi, F. M., and Opella, S. J. (1998) NMR structural studies of membrane proteins, Curr. Opin. Struct. Biol. 8, 640-648.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 640-648
    • Marassi, F.M.1    Opella, S.J.2
  • 30
    • 0032497922 scopus 로고    scopus 로고
    • Multiple states of β-sheet peptide protegrin in lipid bilayers
    • Heller, W. T., Waring, A. J., Lehrer, R. I., and Huang, H. W. (1998) Multiple states of β-sheet peptide protegrin in lipid bilayers, Biochemistry 37, 17331-17338.
    • (1998) Biochemistry , vol.37 , pp. 17331-17338
    • Heller, W.T.1    Waring, A.J.2    Lehrer, R.I.3    Huang, H.W.4
  • 31
    • 0036228299 scopus 로고    scopus 로고
    • An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies
    • Hallock, K. J., Henzler Wildman, K., Lee, D. K., and Ramamoorthy, A. (2002) An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies, Biophys. J. 82, 2499-2503.
    • (2002) Biophys. J. , vol.82 , pp. 2499-2503
    • Hallock, K.J.1    Henzler Wildman, K.2    Lee, D.K.3    Ramamoorthy, A.4
  • 32
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi, S., Huster, D., Waring, A., Lehrer, R. I., Kearney, W., Tack, B. F., and Hong, M. (2001) Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy, Biophys. J. 81, 2203-2214.
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 33
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4554.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4554
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 36
    • 0025101067 scopus 로고
    • Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D
    • Moll, F., III, and Cross, T. A. (1990) Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D, Biophys. J. 57, 351-362.
    • (1990) Biophys. J. , vol.57 , pp. 351-362
    • Moll III, F.1    Cross, T.A.2
  • 39
    • 0001125152 scopus 로고
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR, J. Am. Chem. Soc. 117, 6148-6149.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6148-6149
    • Wu, C.H.1    Ramamoorthy, A.2    Gierasch, L.M.3    Opella, S.J.4
  • 42
    • 0019887621 scopus 로고
    • 31P NMR of hexagonal and isotropic phospholipid phases
    • 31P NMR of hexagonal and isotropic phospholipid phases, Biochemistry 20, 6831.
    • (1981) Biochemistry , vol.20 , pp. 6831
    • Thayer, A.M.1    Kohler, S.J.2
  • 44
    • 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., and Hong, M. (2002) Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study, Biochim. Biophys. Acta 1561, 159-170.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 159-170
    • Huster, D.1    Yao, X.2    Jakes, K.3    Hong, M.4
  • 48
  • 50
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbor effects, J. Biomol. NMR 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 53
    • 0029122152 scopus 로고
    • Influence of transbilayer area asymmetry on the morphology of large unilamellar vesicles
    • Mui, B. L. S., Dobereiner, H. G., Madden, T. D., and Cullis, P. R. (1995) Influence of transbilayer area asymmetry on the morphology of large unilamellar vesicles, Biophys. J. 69, 930-941.
    • (1995) Biophys. J. , vol.69 , pp. 930-941
    • Mui, B.L.S.1    Dobereiner, H.G.2    Madden, T.D.3    Cullis, P.R.4
  • 55
  • 56
    • 0020747256 scopus 로고
    • Formation of tubules by a polymerizable surfactant
    • Yager, P., and Schoen, P. E. (1984) Formation of tubules by a polymerizable surfactant, Mol. Cryst. Liq. Cryst. 106, 371-381.
    • (1984) Mol. Cryst. Liq. Cryst. , vol.106 , pp. 371-381
    • Yager, P.1    Schoen, P.E.2
  • 57
    • 0028284663 scopus 로고
    • Diacetylenic lipid tubules: Experimental evidence for a chiral molecular architecture
    • Schnur, J. M., Ratna, B. R., Selinger, J. V., Singh, A., Jyothi, G., and Eastwaran, K. R. K. (1994) Diacetylenic lipid tubules: experimental evidence for a chiral molecular architecture, Science 264, 945-947.
    • (1994) Science , vol.264 , pp. 945-947
    • Schnur, J.M.1    Ratna, B.R.2    Selinger, J.V.3    Singh, A.4    Jyothi, G.5    Eastwaran, K.R.K.6
  • 58
    • 0026416048 scopus 로고
    • Self-assembling phospholipid filaments
    • Rudolph, A. S., Ratna, B. R., and Kahn, B. (1991) Self-assembling phospholipid filaments, Nature 352, 52-55.
    • (1991) Nature , vol.352 , pp. 52-55
    • Rudolph, A.S.1    Ratna, B.R.2    Kahn, B.3
  • 59
    • 0037123741 scopus 로고    scopus 로고
    • Elongated supramolecular assemblies in drug delivery
    • Zarif, L. (2002) Elongated supramolecular assemblies in drug delivery, J. Controlled Release 81, 7-23.
    • (2002) J. Controlled Release , vol.81 , pp. 7-23
    • Zarif, L.1
  • 61
    • 0001238795 scopus 로고
    • Theory of spontaneous vesicle formation in surfactant mixtures
    • Safran, S. A., Pincus, P., and Andelman, D. (1990) Theory of spontaneous vesicle formation in surfactant mixtures, Science 248, 354-356.
    • (1990) Science , vol.248 , pp. 354-356
    • Safran, S.A.1    Pincus, P.2    Andelman, D.3
  • 62
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz, M. P., and Singer, S. J. (1974) Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions, Proc. Natl. Acad. Sci. U.S.A. 71, 4457-4461.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 63
    • 0029859611 scopus 로고    scopus 로고
    • Location of cholesterol in model membranes by magic-angle-sample-spinning NMR
    • Villalain, J. (1996) Location of cholesterol in model membranes by magic-angle-sample-spinning NMR, Eur. J. Biochem. 241, 586-593.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 586-593
    • Villalain, J.1


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