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Volumn 353, Issue 4, 2007, Pages 889-894

An ultraviolet photoacoustic spectroscopy study of the interaction between Lys49-phospholipase A2 and amphiphilic molecules

Author keywords

Bothropstoxin I; Difference spectroscopy; Fluorescence; Photoacoustic spectroscopy

Indexed keywords

AMPHOPHILE; AROMATIC COMPOUND; BOTHROPSTOXIN I; DODECYL SULFATE SODIUM; HOMODIMER; MEMBRANE PROTEIN; PHENYLALANINE; PHOSPHOLIPASE A2; SNAKE VENOM; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 33846179660     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.085     Document Type: Article
Times cited : (4)

References (24)
  • 2
    • 0035497619 scopus 로고    scopus 로고
    • Analysis of the ethidium bromide bound to DNA by photoacoustic and FTIR spectroscopy
    • Bugs M.R., and Cornélio M.L. Analysis of the ethidium bromide bound to DNA by photoacoustic and FTIR spectroscopy. Photochem. Photobiol. 74 (2001) 512-520
    • (2001) Photochem. Photobiol. , vol.74 , pp. 512-520
    • Bugs, M.R.1    Cornélio, M.L.2
  • 3
    • 0036618994 scopus 로고    scopus 로고
    • A new biophysics approach using photoacoustic spectroscopy to study the DNA-ethidium bromide interaction
    • Bugs M.R., and Cornélio M.L. A new biophysics approach using photoacoustic spectroscopy to study the DNA-ethidium bromide interaction. Eur. Biophys. J. 31 (2002) 232-240
    • (2002) Eur. Biophys. J. , vol.31 , pp. 232-240
    • Bugs, M.R.1    Cornélio, M.L.2
  • 4
    • 0028972997 scopus 로고
    • Phospholipase A2 myotoxins from Bothrops snake venoms
    • Gutierrez J.M., and Lomonte B. Phospholipase A2 myotoxins from Bothrops snake venoms. Toxicon 33 (1995) 1405-1424
    • (1995) Toxicon , vol.33 , pp. 1405-1424
    • Gutierrez, J.M.1    Lomonte, B.2
  • 5
    • 0030201175 scopus 로고    scopus 로고
    • Phospholipase A2-a structural review
    • Arni R.K., and Ward R.J. Phospholipase A2-a structural review. Toxicon 34 (1996) 827-841
    • (1996) Toxicon , vol.34 , pp. 827-841
    • Arni, R.K.1    Ward, R.J.2
  • 6
    • 0023878851 scopus 로고
    • Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin
    • Homsi-Brandeburgo M.I., Queiroz L.S., Santo-Neto H., Rodrigues-Simioni L., and Giglio J.R. Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin. Toxicon 26 (1988) 615-627
    • (1988) Toxicon , vol.26 , pp. 615-627
    • Homsi-Brandeburgo, M.I.1    Queiroz, L.S.2    Santo-Neto, H.3    Rodrigues-Simioni, L.4    Giglio, J.R.5
  • 7
    • 0037084001 scopus 로고    scopus 로고
    • Active-site mutagenesis of a Lys49-phospholipase A2: biological and membrane-disrupting activities in the absence of catalysis
    • Ward R.J., Chioato L., de Oliveira A.H., Ruller R., and Sa J.M. Active-site mutagenesis of a Lys49-phospholipase A2: biological and membrane-disrupting activities in the absence of catalysis. Biochem. J. 362 (2002) 89-96
    • (2002) Biochem. J. , vol.362 , pp. 89-96
    • Ward, R.J.1    Chioato, L.2    de Oliveira, A.H.3    Ruller, R.4    Sa, J.M.5
  • 8
    • 0031593833 scopus 로고    scopus 로고
    • LYS49 phospholipase A2 myotoxins lyse cell cultures by two distinct mechanisms
    • Fletcher J.E., and Jiang M.S. LYS49 phospholipase A2 myotoxins lyse cell cultures by two distinct mechanisms. Toxicon 36 (1998) 1549-1555
    • (1998) Toxicon , vol.36 , pp. 1549-1555
    • Fletcher, J.E.1    Jiang, M.S.2
  • 9
    • 0026068009 scopus 로고
    • The effect of myotoxins isolated from Bothrops snake venoms on multilamellar liposomes: relationship to phospholipase A2, anticoagulant and myotoxic activities
    • Diaz C., Gutierrez J.M., Lomonte B., and Gene J.A. The effect of myotoxins isolated from Bothrops snake venoms on multilamellar liposomes: relationship to phospholipase A2, anticoagulant and myotoxic activities. Biochim. Biophys. Acta 1070 (1991) 455-460
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 455-460
    • Diaz, C.1    Gutierrez, J.M.2    Lomonte, B.3    Gene, J.A.4
  • 11
    • 0028040204 scopus 로고
    • Phospholipase-like myotoxins induce rapid membrane leakage of non-hydrolyzable ether-lipid liposomes
    • Pedersen J.Z., de Arcuri B.F., Morero R.D., and Rufini S. Phospholipase-like myotoxins induce rapid membrane leakage of non-hydrolyzable ether-lipid liposomes. Biochim. Biophys. Acta 1190 (1994) 177-180
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 177-180
    • Pedersen, J.Z.1    de Arcuri, B.F.2    Morero, R.D.3    Rufini, S.4
  • 12
    • 0032031373 scopus 로고    scopus 로고
    • Crystallographic and spectroscopic characterization of a molecular hinge: conformational changes in bothropstoxin I, a dimeric Lys49-phospholipase A2 homologue
    • da Silva Giotto M.T., Garratt R.C., Oliva G., Mascarenhas Y.P., Giglio J.R., Cintra A.C., de Azevedo Jr. W.F., Arni R.K., and Ward R.J. Crystallographic and spectroscopic characterization of a molecular hinge: conformational changes in bothropstoxin I, a dimeric Lys49-phospholipase A2 homologue. Proteins 30 (1998) 442-454
    • (1998) Proteins , vol.30 , pp. 442-454
    • da Silva Giotto, M.T.1    Garratt, R.C.2    Oliva, G.3    Mascarenhas, Y.P.4    Giglio, J.R.5    Cintra, A.C.6    de Azevedo Jr., W.F.7    Arni, R.K.8    Ward, R.J.9
  • 14
    • 6044233426 scopus 로고    scopus 로고
    • 2+-independent membrane-damaging activity in Lys49-phospholipase A2 promoted by amphiphilic molecules
    • 2+-independent membrane-damaging activity in Lys49-phospholipase A2 promoted by amphiphilic molecules. Biochem. Biophys. Res. Commun. 322 (2004) 364-372
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 364-372
    • Bortoleto-Bugs, R.K.1    Neto, A.A.2    Ward, R.J.3
  • 15
    • 33751267684 scopus 로고    scopus 로고
    • A micelle nucleation model for the interaction of dodecyl sulphate with Lys49-phospholipases A(2)
    • Bortoleto-Bugs R.K., Bugs M.R., Neto A.A., and Ward R.J. A micelle nucleation model for the interaction of dodecyl sulphate with Lys49-phospholipases A(2). Biophys. Chem. 125 (2007) 113-120
    • (2007) Biophys. Chem. , vol.125 , pp. 113-120
    • Bortoleto-Bugs, R.K.1    Bugs, M.R.2    Neto, A.A.3    Ward, R.J.4
  • 16
    • 0001800268 scopus 로고
    • Recent Developments in UV-VIS Spectroscopy
    • Perkampus H.H. (Ed), Springer-Verlag, Berlin Heidelberg
    • Perkampus H.-H. Recent Developments in UV-VIS Spectroscopy. In: Perkampus H.H. (Ed). UV-VIS Spectroscopy and Its Applications (1992), Springer-Verlag, Berlin Heidelberg 101-120
    • (1992) UV-VIS Spectroscopy and Its Applications , pp. 101-120
    • Perkampus, H.-H.1
  • 17
    • 0034816787 scopus 로고    scopus 로고
    • The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the bothropstoxin-I dimer
    • de Oliveira A.H., Giglio J.R., Andriao-Escarso S.H., and Ward R.J. The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the bothropstoxin-I dimer. Biochem. Biophys. Res. Commun. 284 (2001) 1011-1015
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 1011-1015
    • de Oliveira, A.H.1    Giglio, J.R.2    Andriao-Escarso, S.H.3    Ward, R.J.4
  • 18
    • 0037370173 scopus 로고    scopus 로고
    • Chemical denaturation of a homodimeric lysine-49 phospholipase A2: a stable dimer interface and a native monomeric intermediate
    • Ruller R., Ferreira T.L., de Oliveira A.H., and Ward R.J. Chemical denaturation of a homodimeric lysine-49 phospholipase A2: a stable dimer interface and a native monomeric intermediate. Arch. Biochem. Biophys. 411 (2003) 112-120
    • (2003) Arch. Biochem. Biophys. , vol.411 , pp. 112-120
    • Ruller, R.1    Ferreira, T.L.2    de Oliveira, A.H.3    Ward, R.J.4
  • 19
    • 25444519212 scopus 로고    scopus 로고
    • A predominant role for hydrogen bonding in the stability of the homodimer of bothropstoxin-I, a lysine 49-phospholipase A2
    • Ruller R., Aparecida-Aragão E., Chioato L., Ferreira-Lopes T., de Oliveira A.H.C., Sà J.M., and Ward R.J. A predominant role for hydrogen bonding in the stability of the homodimer of bothropstoxin-I, a lysine 49-phospholipase A2. Biochimie 87 (2005) 993-1003
    • (2005) Biochimie , vol.87 , pp. 993-1003
    • Ruller, R.1    Aparecida-Aragão, E.2    Chioato, L.3    Ferreira-Lopes, T.4    de Oliveira, A.H.C.5    Sà, J.M.6    Ward, R.J.7
  • 20
    • 33846150385 scopus 로고    scopus 로고
    • T.E. Creighton, In: Proteins structures and molecular properties. W.H. Freman and Company, New York, 1993, pp. 14-17.
  • 21
    • 0017487123 scopus 로고
    • Resolution of the fluorescence spectrum of indole into the 1La and 1Lb excitation bands
    • Valeur B., and Weber G. Resolution of the fluorescence spectrum of indole into the 1La and 1Lb excitation bands. Photochem. Photobiol. 25 (1977) 441-444
    • (1977) Photochem. Photobiol. , vol.25 , pp. 441-444
    • Valeur, B.1    Weber, G.2
  • 23
    • 33646927210 scopus 로고    scopus 로고
    • Protein-solvent interactions
    • Prabhu N., and Sharp K. Protein-solvent interactions. Chem. Rev. 106 (2006) 1616-1623
    • (2006) Chem. Rev. , vol.106 , pp. 1616-1623
    • Prabhu, N.1    Sharp, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.