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Volumn 36, Issue 2, 2009, Pages 251-260

Non-covalent binding of azo compound to peptide chain: Interactions of biebrich scarlet and naphthochrome green with four model proteins

Author keywords

Azo compound; Conformational change; Molecular spectrometry; Non covalent binding; Protein toxicity; Protein ligand interaction

Indexed keywords

AZO COMPOUND; BOVINE SERUM ALBUMIN; DYE; ELECTROLYTE; HEMOGLOBIN; NAPHTHOCHROME GREEN; OVALBUMIN; PEPTIDE; POLYLYSINE; SCARLET RED; UNCLASSIFIED DRUG;

EID: 59449104195     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-008-0058-1     Document Type: Article
Times cited : (7)

References (28)
  • 1
    • 0033204974 scopus 로고    scopus 로고
    • Fluorescent probes for structural and distance effect studies in micelles, reversed micelles and micromulsions
    • GB Behera BK Mishra PK Behera M Panda 1999 Fluorescent probes for structural and distance effect studies in micelles, reversed micelles and micromulsions Adv Colloid Interface 82 1 42
    • (1999) Adv Colloid Interface , vol.82 , pp. 1-42
    • Behera, G.B.1    Mishra, B.K.2    Behera, P.K.3    Panda, M.4
  • 2
    • 22544454196 scopus 로고    scopus 로고
    • Ligand-regulated peptides: A general approach for modulating protein-peptide interactions with small molecules
    • BF Binkowski RA Miller PJ Belshaw 2005 Ligand-regulated peptides: a general approach for modulating protein-peptide interactions with small molecules Chem Biol 12 847 855
    • (2005) Chem Biol , vol.12 , pp. 847-855
    • Binkowski, B.F.1    Miller, R.A.2    Belshaw, P.J.3
  • 3
    • 3042550172 scopus 로고    scopus 로고
    • Copper-containing amine oxidases, Biogenesis and catalysis: A structural perspective
    • BJ Brazeau BJ Johnson CM Wilmot 2004 Copper-containing amine oxidases, Biogenesis and catalysis: a structural perspective Arch Biochem Biophys 428 22 31
    • (2004) Arch Biochem Biophys , vol.428 , pp. 22-31
    • Brazeau, B.J.1    Johnson, B.J.2    Wilmot, C.M.3
  • 4
    • 1642575136 scopus 로고    scopus 로고
    • Fluorescence spectroscopy studies on 5-aminosalicylic acid and Zin 5-aminosalylicylate interaction with human serum albumin
    • FL Cui J Fan W Li YC Fan ZD Hu 2004 Fluorescence spectroscopy studies on 5-aminosalicylic acid and Zin 5-aminosalylicylate interaction with human serum albumin J Pharm Biomed Anal 34 189 197
    • (2004) J Pharm Biomed Anal , vol.34 , pp. 189-197
    • Cui, F.L.1    Fan, J.2    Li, W.3    Fan, Y.C.4    Hu, Z.D.5
  • 5
    • 0034602966 scopus 로고    scopus 로고
    • Conformational transitions of the three recombinant domains of human serum albumin depending on pH
    • M Dockal DC Carter F Rüker 2000 Conformational transitions of the three recombinant domains of human serum albumin depending on pH J Biol Chem 275 3042 3050
    • (2000) J Biol Chem , vol.275 , pp. 3042-3050
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3
  • 6
    • 50549181757 scopus 로고
    • Two new staining procedures for quantitative estimation of proteins on electrophoretic strips
    • GS Fazekas RG Webster A Datyner 1963 Two new staining procedures for quantitative estimation of proteins on electrophoretic strips Biochim Biophys Acta 1 377 391
    • (1963) Biochim Biophys Acta , vol.1 , pp. 377-391
    • Fazekas, G.S.1    Webster, R.G.2    Datyner, A.3
  • 8
    • 0344861854 scopus 로고    scopus 로고
    • Interaction of spectral probe with biomacromolecule: Satranin T-nucleic acid assembly
    • HW Gao JF Zhao 2003 Interaction of spectral probe with biomacromolecule: satranin T-nucleic acid assembly J Trace Microprob T 21 615 625
    • (2003) J Trace Microprob T , vol.21 , pp. 615-625
    • Gao, H.W.1    Zhao, J.F.2
  • 9
    • 27744459448 scopus 로고    scopus 로고
    • Interactions of modified mono- and bis-β-cyclodextrins with bovine serum albumin
    • H Gao YN Wang YG Fan JB Ma 2006 Interactions of modified mono- and bis-β-cyclodextrins with bovine serum albumin Bioorg Med Chem 14 131 137
    • (2006) Bioorg Med Chem , vol.14 , pp. 131-137
    • Gao, H.1    Wang, Y.N.2    Fan, Y.G.3    Ma, J.B.4
  • 10
    • 33749615684 scopus 로고    scopus 로고
    • Non-covalent Interaction of 2′, 4′, 5′, 7′-tetrabromo-4, 5, 6, 7-tetrachlorofluorescein with proteins and its application
    • HW Gao JF Zhao QZ Yang XH Liu L Chen LT Pan 2006 Non-covalent Interaction of 2′, 4′, 5′, 7′-tetrabromo-4, 5, 6, 7-tetrachlorofluorescein with proteins and its application Proteomics 6 5140 151
    • (2006) Proteomics , vol.6 , pp. 5140-5151
    • Gao, H.W.1    Zhao, J.F.2    Yang, Q.Z.3    Liu, X.H.4    Chen, L.5    Pan, L.T.6
  • 11
    • 20444415980 scopus 로고    scopus 로고
    • Immobilisation of a repressor protein for binding of plasmid DNA
    • AA Hasche C Voss 2005 Immobilisation of a repressor protein for binding of plasmid DNA J Chromatogr A 1080 76 82
    • (2005) J Chromatogr A , vol.1080 , pp. 76-82
    • Hasche, A.A.1    Voss, C.2
  • 12
    • 0033072718 scopus 로고    scopus 로고
    • Pharmacogenetics of cytochromes P450
    • JA Hasler 1999 Pharmacogenetics of cytochromes P450 Mol Aspects Med 20 12 24
    • (1999) Mol Aspects Med , vol.20 , pp. 12-24
    • Hasler, J.A.1
  • 13
    • 12344337543 scopus 로고    scopus 로고
    • Peptide ligand binding properties of the corticotropin-releasing factor (CRF) type 2 receptor: Pharmacology of endogenously expressed receptors, G-protein-coupling sensitivity and determinants of CRF2 receptor selectivity
    • SRJ Hoare SK Sullivan J Fan K Khongsaly DE Grigoriadis 2005 Peptide ligand binding properties of the corticotropin-releasing factor (CRF) type 2 receptor: pharmacology of endogenously expressed receptors, G-protein-coupling sensitivity and determinants of CRF2 receptor selectivity Peptide 26 457 470
    • (2005) Peptide , vol.26 , pp. 457-470
    • Hoare, S.R.J.1    Sullivan, S.K.2    Fan, J.3    Khongsaly, K.4    Grigoriadis, D.E.5
  • 15
    • 16244366490 scopus 로고    scopus 로고
    • Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e
    • CF Lee MD Allen M Bycroft KB Wong 2005 Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e J Mol Biol 348 419 431
    • (2005) J Mol Biol , vol.348 , pp. 419-431
    • Lee, C.F.1    Allen, M.D.2    Bycroft, M.3    Wong, K.B.4
  • 16
    • 34548273489 scopus 로고    scopus 로고
    • A highly selective colorimetric chemosensor for detecting the respective amounts of iron(II) and iron(III) ions in water
    • ZQ Liang CX Wang JX Yang HW Gao YP Tian XT Tao MH Jiang 2007 A highly selective colorimetric chemosensor for detecting the respective amounts of iron(II) and iron(III) ions in water New J Chem 31 906 910
    • (2007) New J Chem , vol.31 , pp. 906-910
    • Liang, Z.Q.1    Wang, C.X.2    Yang, J.X.3    Gao, H.W.4    Tian, Y.P.5    Tao, X.T.6    Jiang, M.H.7
  • 17
    • 33745274177 scopus 로고    scopus 로고
    • Inhibition of human tyrosyl-DNA phosphodiesterase by aminoglycoside antibiotics and ribosome inhibitors
    • ZY Liao L Thibaut A Jobson Y Pommier 2006 Inhibition of human tyrosyl-DNA phosphodiesterase by aminoglycoside antibiotics and ribosome inhibitors Mol Pharmacol 70 366 372
    • (2006) Mol Pharmacol , vol.70 , pp. 366-372
    • Liao, Z.Y.1    Thibaut, L.2    Jobson, A.3    Pommier, Y.4
  • 19
    • 0033040625 scopus 로고    scopus 로고
    • Enhancement in the lysozyme activity of the hen egg white foam matrix by cross-linking in the presence of N-acetyl glucosamine
    • KZ Marolia SF D'Souza 1999 Enhancement in the lysozyme activity of the hen egg white foam matrix by cross-linking in the presence of N-acetyl glucosamine J Biochem Biophys Methods 39 115 117
    • (1999) J Biochem Biophys Methods , vol.39 , pp. 115-117
    • Marolia, K.Z.1    D'Souza, S.F.2
  • 20
  • 21
    • 59449090221 scopus 로고
    • Oxford University Press New York
    • Patrick GL (1995) An introduction to medicinal chemistry. Oxford University Press, New York, pp 78-80
    • (1995) , pp. 78-80
    • Patrick, G.L.1
  • 22
    • 33748893018 scopus 로고    scopus 로고
    • Interactions between neurotensin receptors and G proteins
    • D Pelaprat 2006 Interactions between neurotensin receptors and G proteins Peptides 27 2476 2487
    • (2006) Peptides , vol.27 , pp. 2476-2487
    • Pelaprat, D.1
  • 23
    • 0030018067 scopus 로고    scopus 로고
    • Congo red-stabilized. intermediates in the λ light chain transition from native to molten state
    • B Piekarska M Skowronek J Rybarska B Stopa I Roterman L Konieczny 1996 Congo red-stabilized. intermediates in the λ light chain transition from native to molten state Biochimie 78 183 189
    • (1996) Biochimie , vol.78 , pp. 183-189
    • Piekarska, B.1    Skowronek, M.2    Rybarska, J.3    Stopa, B.4    Roterman, I.5    Konieczny, L.6
  • 24
    • 0024341102 scopus 로고
    • Selective inhibition of cytokine-induced lysozyme activity by tetanus toxin in the GG2EE macrophage cell line
    • L Pitzurra P Marconi F Bistoni E Blasi 1989 Selective inhibition of cytokine-induced lysozyme activity by tetanus toxin in the GG2EE macrophage cell line Infect Immun 57 2452 2456
    • (1989) Infect Immun , vol.57 , pp. 2452-2456
    • Pitzurra, L.1    Marconi, P.2    Bistoni, F.3    Blasi, E.4
  • 25
    • 14844302394 scopus 로고    scopus 로고
    • Functional interaction of protein kinase C alpha with the tyrosine kinases Syk and Src in human platelets
    • G Pula D Crosby J Baker AW Poole 2005 Functional interaction of protein kinase C alpha with the tyrosine kinases Syk and Src in human platelets J Biol Chem 280 7194 7205
    • (2005) J Biol Chem , vol.280 , pp. 7194-7205
    • Pula, G.1    Crosby, D.2    Baker, J.3    Poole, A.W.4
  • 28
    • 22544445805 scopus 로고    scopus 로고
    • Study on the interaction between chlortetracycline and bovine serum albumin
    • PG Yi QS Yu ZC Shang M Guo 2003 Study on the interaction between chlortetracycline and bovine serum albumin Chin J Chem Phys 16 420 425
    • (2003) Chin J Chem Phys , vol.16 , pp. 420-425
    • Yi, P.G.1    Yu, Q.S.2    Shang, Z.C.3    Guo, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.