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Volumn 1784, Issue 6, 2008, Pages 924-929

Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif

Author keywords

Antimicrobial; Molecular modelling; NMR; Ranatuerin 2

Indexed keywords

ALANINE; ASPARTIC ACID; GLYCINE; HELIX LOOP HELIX PROTEIN; ISOLEUCINE; LEUCINE; LYSINE; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT; RANATUERIN 2CSA; SERINE; SOLVENT; TRIFLUOROETHANOL; VALINE; WATER;

EID: 43649109015     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.02.019     Document Type: Article
Times cited : (28)

References (34)
  • 1
    • 12944302098 scopus 로고    scopus 로고
    • Lack of development of new antimicrobial drugs: a potential serious threat to public health
    • Norrby S.R., Nord C.E., and Finch R. Lack of development of new antimicrobial drugs: a potential serious threat to public health. Lancet Infect. Dis. 5 (2005) 115-119
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 115-119
    • Norrby, S.R.1    Nord, C.E.2    Finch, R.3
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1 (2001) 156-164
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 3
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff M., Martin B., and Chen H.C. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 910-913
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.C.3
  • 4
    • 3242717490 scopus 로고    scopus 로고
    • The therapeutic potential of antimicrobial peptides from frog skin
    • Conlon J.M. The therapeutic potential of antimicrobial peptides from frog skin. Rev. Med. Micro. 15 (2004) 17-25
    • (2004) Rev. Med. Micro. , vol.15 , pp. 17-25
    • Conlon, J.M.1
  • 5
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon J.M., Kolodziejek J., and Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim. Biophys. Acta 1696 (2004) 1-14
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 6
    • 0032578602 scopus 로고    scopus 로고
    • Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana
    • Goraya J., Knoop F.C., and Conlon J.M. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Biochem. Biophys. Res. Commun. 250 (1998) 589-592
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 589-592
    • Goraya, J.1    Knoop, F.C.2    Conlon, J.M.3
  • 9
    • 0003062277 scopus 로고
    • Simplification of NMR spectra by filtration through multiple-quantum coherence
    • Shaka A.J., and Freeman R. Simplification of NMR spectra by filtration through multiple-quantum coherence. J. Magn. Reson. 51 (1983) 169-173
    • (1983) J. Magn. Reson. , vol.51 , pp. 169-173
    • Shaka, A.J.1    Freeman, R.2
  • 10
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetisation transfer spectroscopy
    • Bax A., and Davis D.G. MLEV-17 based two-dimensional homonuclear magnetisation transfer spectroscopy. J. Magn. Reson. 65 (1985) 355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 11
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., and Wüthrich K. A two-dimensional nuclear Overhauser enhancement experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95 (1980) 1-6
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 13
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P., Braun W., and Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217 (1991) 517-530
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 14
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P., Mumenthaler C., and Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 15
    • 43649104565 scopus 로고    scopus 로고
    • Tripos. St. Louis, MO 63144-2319, USA: Inc., 1699 South Janley Road.
    • Tripos. St. Louis, MO 63144-2319, USA: Inc., 1699 South Janley Road.
  • 16
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 51-5 (1996) 29-32
    • (1996) J. Mol. Graph. , vol.14 , Issue.51-5 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 17
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmann J.A.C., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 18
    • 34249932868 scopus 로고    scopus 로고
    • Bioactive conformation of glucose-dependent insulinotropic polypeptide by NMR and CD spectroscopy, PROTEINS: structure
    • Alana I., Malthouse J.P.G., O'Harte F.P., and Hewage C.M. Bioactive conformation of glucose-dependent insulinotropic polypeptide by NMR and CD spectroscopy, PROTEINS: structure. Func. and Bioinfor. 68 (2007) 92-99
    • (2007) Func. and Bioinfor. , vol.68 , pp. 92-99
    • Alana, I.1    Malthouse, J.P.G.2    O'Harte, F.P.3    Hewage, C.M.4
  • 19
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 20
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers, 66 (2002) 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 21
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers J.P., and Hancock R.E. The relationship between peptide structure and antibacterial activity. Peptides 24 (2003) 1681-1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 22
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 23
    • 34249806711 scopus 로고    scopus 로고
    • Strategies for development of naturally occurring antimicrobial peptides into therapeutically valuable anti-infective agents
    • Conlon J.M., Al-Ghaferi N., Abraham B., and Leprince J. Strategies for development of naturally occurring antimicrobial peptides into therapeutically valuable anti-infective agents. Methods 42 (2007) 349-357
    • (2007) Methods , vol.42 , pp. 349-357
    • Conlon, J.M.1    Al-Ghaferi, N.2    Abraham, B.3    Leprince, J.4
  • 24
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 25
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study
    • Holak T.A., Engstrom A., Kraulis P.J., Lindeberg G., Bennich H., Jones T.A., Gronenborn A.M., and Clore G.M. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27 (1988) 7620-7629
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engstrom, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 26
    • 1542289126 scopus 로고    scopus 로고
    • Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its [Lys-8]-substituted analog
    • Sonnevend A., Knoop F.C., Patel M., Pál T., Soto A.M., and Conlon J.M. Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its [Lys-8]-substituted analog. Peptides 25 (2004) 29-36
    • (2004) Peptides , vol.25 , pp. 29-36
    • Sonnevend, A.1    Knoop, F.C.2    Patel, M.3    Pál, T.4    Soto, A.M.5    Conlon, J.M.6
  • 28
    • 33748919831 scopus 로고    scopus 로고
    • Membrane interactions of antimicrobial peptides from Australian tree frogs
    • Boland M.P., and Separovic F. Membrane interactions of antimicrobial peptides from Australian tree frogs. Biochim. Biophys. Acta. 1758 (2006) 1178-1183
    • (2006) Biochim. Biophys. Acta. , vol.1758 , pp. 1178-1183
    • Boland, M.P.1    Separovic, F.2
  • 29
    • 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., and Sykes B.D. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31 (1992) 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
  • 30
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff A., and Fersht A.R. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33 (1994) 2129-2135
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 31
    • 0033005130 scopus 로고    scopus 로고
    • A linear endothelin-1 analogue: solution structure of ET-1[Aib1,3,11,15, Nle7] by nuclear magnetic resonance spectroscopy and molecular modelling
    • Hewage C.M., Jiang L., Parkinson J.A., Ramage R., and Sadler I.H. A linear endothelin-1 analogue: solution structure of ET-1[Aib1,3,11,15, Nle7] by nuclear magnetic resonance spectroscopy and molecular modelling. Neurochem. Int. 35 (1999) 35-45
    • (1999) Neurochem. Int. , vol.35 , pp. 35-45
    • Hewage, C.M.1    Jiang, L.2    Parkinson, J.A.3    Ramage, R.4    Sadler, I.H.5
  • 32
    • 0028838504 scopus 로고
    • Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor
    • Kemmink J., and Creighton T.E. Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor. Biochemistry 34 (1995) 12630-12635
    • (1995) Biochemistry , vol.34 , pp. 12630-12635
    • Kemmink, J.1    Creighton, T.E.2
  • 33
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding
    • Shiraki K., Nishikawa K., and Goto Y. Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245 (1995) 180-194
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 34
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide
    • Sonnichsen F.D., Van Eyk J.E., Hodges R.S., and Sykes B.D. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31 (1992) 8790-8798
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4


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