메뉴 건너뛰기




Volumn 309, Issue 3, 2003, Pages 591-597

Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy

Author keywords

Antimicrobial activity; CD spectra; NMR spectroscopy; Spinigerin; Helix

Indexed keywords

HISTIDYLVALYLASPARTYLLYSYLLYSYLVALYLALANYLASPARTYLLYSYLVALYLLEUCYLLEUCYL LEU CYLLYSYLGLUTAMINYLLEUCYLARGINYLISOLEUCYLMETHIONYLARGINYLLEUCYLLEUCYLTHREONYLARGI NYLLEUCINE; ANTIINFECTIVE AGENT; ARGININE; DODECYL SULFATE SODIUM; LEUCINE; LYSINE; PEPTIDE DERIVATIVE; PHOSPHOLIPID DERIVATIVE; SPINIGERIN; THREONINE; UNCLASSIFIED DRUG;

EID: 0042330422     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.08.043     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0033515629 scopus 로고    scopus 로고
    • Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity
    • Lamberty M., Ades S., Uttenweiler-Joseph S., Brookhart G., Bushey D., Hoffmann J.A., Bulet P. Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. J. Biol. Chem. 274:1997;9320-9326.
    • (1997) J. Biol. Chem. , vol.274 , pp. 9320-9326
    • Lamberty, M.1    Ades, S.2    Uttenweiler-Joseph, S.3    Brookhart, G.4    Bushey, D.5    Hoffmann, J.A.6    Bulet, P.7
  • 2
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13:1995;61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 3
    • 0035830902 scopus 로고    scopus 로고
    • Insect Immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect
    • Lamberty M., Zachary D., Lanot R., Bordereau C., Robert A., Hoffmann J.A., Bulet P. Insect Immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect. J. Biol. Chem. 276:2001;4085-4092.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4085-4092
    • Lamberty, M.1    Zachary, D.2    Lanot, R.3    Bordereau, C.4    Robert, A.5    Hoffmann, J.A.6    Bulet, P.7
  • 4
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield R.B. Solid phase synthesis. Science. 232:1986;341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 5
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J., Cho Y., Dinh N.N., Waring A.J., Lehrer R.I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42:1998;2206-2214.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 6
    • 0033063075 scopus 로고    scopus 로고
    • In vitro activities of designed antimicrobial peptides against multidrug-resistant cystic fibrosis pathogens
    • Schwab U., Gilligan P., Jaynes J., Henke D. In vitro activities of designed antimicrobial peptides against multidrug-resistant cystic fibrosis pathogens. Antimicrob. Agents Chemother. 43:1999;1435-1440.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1435-1440
    • Schwab, U.1    Gilligan, P.2    Jaynes, J.3    Henke, D.4
  • 7
    • 0033974530 scopus 로고    scopus 로고
    • Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells
    • Shin S.Y., Kang J.H., Jang S.Y., Kim Y., Kim K.L., Hahm K.S. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim. Biophys. Acta. 1463:2000;209-218.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 209-218
    • Shin, S.Y.1    Kang, J.H.2    Jang, S.Y.3    Kim, Y.4    Kim, K.L.5    Hahm, K.S.6
  • 8
    • 44949290287 scopus 로고
    • Rapid-pulsing artifacts in double-quantum-filtered COSY
    • Derome A., Williamson M. Rapid-pulsing artifacts in double-quantum-filtered COSY. J. Magn. Reson. 88:1990;177-185.
    • (1990) J. Magn. Reson. , vol.88 , pp. 177-185
    • Derome, A.1    Williamson, M.2
  • 9
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization 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
  • 10
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura S., Ernst R.R. Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41:1980;95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 11
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax A., Davis D.G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:1985;207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 13
    • 45949127312 scopus 로고
    • P.E.COSY, a simple alternative to E.COSY
    • Muller L. P.E.COSY, a simple alternative to E.COSY. J. Magn. Reson. 72:1987;191-197.
    • (1987) J. Magn. Reson. , vol.72 , pp. 191-197
    • Muller, L.1
  • 14
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Skenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-666.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-666
    • Piotto, M.1    Saudek, V.2    Skenar, V.3
  • 15
    • 45249128810 scopus 로고
    • Measurement of vicinal coupling from cross peaks in COSY spectra
    • Kim Y., Prestegard J.P. Measurement of vicinal coupling from cross peaks in COSY spectra. J. Magn. Reson. 84:1989;9-13.
    • (1989) J. Magn. Reson. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.P.2
  • 17
    • 0024351231 scopus 로고
    • Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy
    • Clore G.M., Gronenborn A.M. Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. Biol. 24:1989;479-564.
    • (1989) CRC Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 479-564
    • Clore, G.M.1    Gronenborn, A.M.2
  • 18
    • 0028389672 scopus 로고
    • Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR
    • Clore G.M., Gronenborn A.M. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR. Protein Sci. 3:1994;372-390.
    • (1994) Protein Sci. , vol.3 , pp. 372-390
    • Clore, G.M.1    Gronenborn, A.M.2
  • 20
    • 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. 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. 169:1983;949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 21
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore G.M., Gronenborn A.M., Nilges M., Ryan C.A. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry. 26:1987;8012-8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 22
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges M., Clore G.M., Gronenborn A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229:1988;317-324.
    • (1988) FEBS Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 23
    • 0026676167 scopus 로고
    • Sampling and efficiency of metric matrix distance geometry:a novel partial metrization algorithm
    • Kuszewski J., Nilges M., Brünger A.T. Sampling and efficiency of metric matrix distance geometry:a novel partial metrization algorithm. J. Biomol. NMR. 2:1992;33-56.
    • (1992) J. Biomol. NMR , vol.2 , pp. 33-56
    • Kuszewski, J.1    Nilges, M.2    Brünger, A.T.3
  • 25
    • 0026597879 scopus 로고
    • The chemical shift index:a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., Richards F.M. The chemical shift index:a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1992;1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.