메뉴 건너뛰기




Volumn 247, Issue 2, 1997, Pages 545-557

The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida

Author keywords

Amphipathic helix; Antimicrobial peptide; NMR; Solution structure

Indexed keywords

ANTIINFECTIVE AGENT; PEPTIDE;

EID: 0030852756     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00545.x     Document Type: Article
Times cited : (127)

References (48)
  • 2
    • 0029047938 scopus 로고
    • Amphibian skin: A promising resource for antimicrobial peptides
    • Barra, D. & Simmaco, M. (1995) Amphibian skin: a promising resource for antimicrobial peptides, Trends Biotech. 13, 205-209.
    • (1995) Trends Biotech. , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 5
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., Zasloff, M. & 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
  • 7
    • 0031128030 scopus 로고    scopus 로고
    • Structural basis between retro-inverso and parent peptides. Molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from footand-mouth disease virus
    • Carver, J. A., Esposito, G., Viglino, P., Fogolari, F., Guichard, G., Briand, J.-P., Van Regenmortel, M. H. V., Brown, F. & Mascagni, P. (1997) Structural basis between retro-inverso and parent peptides. Molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from footand-mouth disease virus, Biopolymers 41, 569-590.
    • (1997) Biopolymers , vol.41 , pp. 569-590
    • Carver, J.A.1    Esposito, G.2    Viglino, P.3    Fogolari, F.4    Guichard, G.5    Briand, J.-P.6    Van Regenmortel, M.H.V.7    Brown, F.8    Mascagni, P.9
  • 8
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy, J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 9
    • 0000952847 scopus 로고
    • Bioactive secretions of the amphibian integument
    • Surrey Beatty, Chipping Norton, Australia
    • Erspamer, V. (1994) Bioactive secretions of the amphibian integument, in Amphibian biology. The integument, vol. 1, pp. 178-350, Surrey Beatty, Chipping Norton, Australia.
    • (1994) Amphibian Biology. The Integument , vol.1 , pp. 178-350
    • Erspamer, V.1
  • 13
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel, T. F. (1991) An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance, Prog. Biophys. Mol. Biol. 56, 43-78.
    • (1991) Prog. Biophys. Mol. Biol. , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 14
    • 0029930324 scopus 로고    scopus 로고
    • Secondary structure of an armadillo single repeat from the APC protein
    • Hirschl, D., Bayer, P. & Müller, O. (1996) Secondary structure of an armadillo single repeat from the APC protein, FEBS Lett. 383, 31-36.
    • (1996) FEBS Lett. , vol.383 , pp. 31-36
    • Hirschl, D.1    Bayer, P.2    Müller, O.3
  • 15
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: A nuclear magnetic resonance and dynamical simulated annealing study
    • Holak, T. A., Engström, Å., Kraulis, P. J., Lindeberg, G., Bennich, H., Jones, T. A., Gronenborn, A. M. & Clore, G. M. (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study, Biochemistry 27, 7620-7629.
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engström, Å.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 17
    • 0028721118 scopus 로고
    • Potential therapeutic applications of magainins and other antimicrobial agents of animal origin
    • Jacob, L. & Zasloff, M. (1994) Potential therapeutic applications of magainins and other antimicrobial agents of animal origin, Ciba Found. Symp. 186, 197-223.
    • (1994) Ciba Found. Symp. , vol.186 , pp. 197-223
    • Jacob, L.1    Zasloff, M.2
  • 18
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachman, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 19
    • 44049117096 scopus 로고
    • Effective combination of gradients and crafted RF pulses for water suppression in biological samples
    • John, B. K., Plant, D., Webb, P. & Hurd, R. E. (1992) Effective combination of gradients and crafted RF pulses for water suppression in biological samples, J. Magn. Reson. 98, 200-206.
    • (1992) J. Magn. Reson. , vol.98 , pp. 200-206
    • John, B.K.1    Plant, D.2    Webb, P.3    Hurd, R.E.4
  • 21
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P. & Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 22
    • 0000802107 scopus 로고
    • (Sneath, P. H. A., ed.) Williams and Wilkins, Baltimore MD
    • Kocur, M. (1986) in Bergey's manual of systematic bacteriology, vol. 2 (Sneath, P. H. A., ed.) pp. 1004-1008, Williams and Wilkins, Baltimore MD.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1004-1008
    • Kocur, M.1
  • 23
    • 0001093747 scopus 로고
    • Spectroscopic studies of alcohols. III Fundamental OH stretching bands of 2,2-di- and 2.2,2-tri-haloethanols
    • Krueger, P. J. & Mettee, H. D. (1964) Spectroscopic studies of alcohols. III Fundamental OH stretching bands of 2,2-di- and 2.2,2-tri-haloethanols, Can. J. Chem. 42, 340-346.
    • (1964) Can. J. Chem. , vol.42 , pp. 340-346
    • Krueger, P.J.1    Mettee, H.D.2
  • 26
    • 0023875642 scopus 로고
    • A two-dimensional NMR study of the antimicrobial peptide magainin 2
    • Marion, D., Zasloff, M. & Bax, A. (1988) A two-dimensional NMR study of the antimicrobial peptide magainin 2, FEBS Lett. 227, 21-26.
    • (1988) FEBS Lett. , vol.227 , pp. 21-26
    • Marion, D.1    Zasloff, M.2    Bax, A.3
  • 27
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG, J. Biomol. NMR 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 28
    • 0001202015 scopus 로고
    • The relationship between chemical shift and secondary structure
    • Pastore, A. & Saudek, V. (1990) The relationship between chemical shift and secondary structure, J. Magn. Reson. 90, 165-176.
    • (1990) J. Magn. Reson. , vol.90 , pp. 165-176
    • Pastore, A.1    Saudek, V.2
  • 29
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta, L. G. & Rose, G. D. (1988) Helix signals in proteins, Science 240, 1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 30
    • 0029398795 scopus 로고
    • Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers
    • Ramamoorthy, A., Marassi, F. M., Zasloff, M. & Opella, S. J. (1995) Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers. J. Biomol. NMR 6, 329-334.
    • (1995) J. Biomol. NMR , vol.6 , pp. 329-334
    • Ramamoorthy, A.1    Marassi, F.M.2    Zasloff, M.3    Opella, S.J.4
  • 32
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson, J. S. & Richardson, D. C. (1988) Amino acid preferences for specific locations at the ends of α helices, Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 33
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. (1995) Molecular recognition between membrane-spanning polypeptides, Trends Biochem. Sci. 20, 460-464.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 34
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., Van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide, Biochemistry 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 37
    • 37049090262 scopus 로고
    • Peptides from Australian frogs. Structures of the caerins and caeridin 1 from Litoria splendida
    • Stone, D. J. M., Waugh, R. J., Bowie, J. H., Wallace, J. C. & Tyler, M. J. (1992b) Peptides from Australian frogs. Structures of the caerins and caeridin 1 from Litoria splendida, J. Chem. Soc. Perkin Trans. 1, 3173-3178.
    • (1992) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 3173-3178
    • Stone, D.J.M.1    Waugh, R.J.2    Bowie, J.H.3    Wallace, J.C.4    Tyler, M.J.5
  • 38
    • 0001523424 scopus 로고
    • Peptides from Australian frogs. The structures of the caerins from Litoria caerulea
    • Stone, D. J. M., Waugh, R. J., Bowie, J. H., Wallace, J. C. & Tyler, J. C. (1993) Peptides from Australian frogs. The structures of the caerins from Litoria caerulea, J. Chem. Res. 138, 910-936.
    • (1993) J. Chem. Res. , vol.138 , pp. 910-936
    • Stone, D.J.M.1    Waugh, R.J.2    Bowie, J.H.3    Wallace, J.C.4    Tyler, J.C.5
  • 39
    • 0027006857 scopus 로고
    • Helix propagation in trifluoroethanol solutions
    • Storrs, R. W., Truckses, D. & Wemmer, D. E. (1992) Helix propagation in trifluoroethanol solutions, Biopolymers 32, 1695-1702.
    • (1992) Biopolymers , vol.32 , pp. 1695-1702
    • Storrs, R.W.1    Truckses, D.2    Wemmer, D.E.3
  • 40
    • 0009700971 scopus 로고
    • Peptides from Australian frogs. The structures of the caerins and caeridins from Litoria gilleni
    • Waugh, R. J., Stone, D. J. M., Bowie, J. H., Wallace, J. C. & Tyler, M. J. (1993) Peptides from Australian frogs. The structures of the caerins and caeridins from Litoria gilleni, J. Chem. Res. 139, 937-961.
    • (1993) J. Chem. Res. , vol.139 , pp. 937-961
    • Waugh, R.J.1    Stone, D.J.M.2    Bowie, J.H.3    Wallace, J.C.4    Tyler, M.J.5
  • 41
    • 0000265959 scopus 로고
    • Two isomeric α and β aspartyl dodecapeptides and their cyclic amino succinyl analogue from the Australian green tree frog Litoria gilleni
    • Waugh, R. J., Steinborner, S. T., Bowie, J. H., Wallace, J. C., Tyler, M. J., Hu, P. & Gross, M. L. (1995) Two isomeric α and β aspartyl dodecapeptides and their cyclic amino succinyl analogue from the Australian green tree frog Litoria gilleni, Aust. J. Chem. 48, 1981-1987.
    • (1995) Aust. J. Chem. , vol.48 , pp. 1981-1987
    • Waugh, R.J.1    Steinborner, S.T.2    Bowie, J.H.3    Wallace, J.C.4    Tyler, M.J.5    Hu, P.6    Gross, M.L.7
  • 42
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 43
    • 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
  • 44
    • 0025602520 scopus 로고
    • The influence of proline residues on α-helical structure
    • Woolfson, D. N. & Williams, D. H. (1990) The influence of proline residues on α-helical structure. FEBS Lett. 277, 185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 46
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K., Billeter, M. & Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance, J. Mol. Biol. 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 47
    • 0030602175 scopus 로고    scopus 로고
    • Solution structure of an antimicrobial peptide buforin II
    • Yi, G.-S., Park, C. B., Kim, S. C. & Cheong, C. (1996) Solution structure of an antimicrobial peptide buforin II, FEBS Lett. 398, 87-90.
    • (1996) FEBS Lett. , vol.398 , pp. 87-90
    • Yi, G.-S.1    Park, C.B.2    Kim, S.C.3    Cheong, C.4
  • 48
    • 84990461819 scopus 로고
    • 1H-NMR methyl lines and conformation of valyl residues in the lac repressor headpiece
    • 1H-NMR methyl lines and conformation of valyl residues in the lac repressor headpiece. Biopolymers 24, 601-611.
    • (1985) Biopolymers , vol.24 , pp. 601-611
    • Zuiderweg, E.R.P.1    Boelens, R.2    Kaptein, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.