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Volumn 8, Issue 10, 2013, Pages

Investigation of Human Albumin-Induced Circular Dichroism in Dansylglycine

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; DANSYLGLYCINE; GLYCINE; HUMAN SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 84885789435     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0076849     Document Type: Article
Times cited : (50)

References (40)
  • 2
    • 79952446257 scopus 로고    scopus 로고
    • Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin
    • Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S, (2011) Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol 174(1): 84-91.
    • (2011) J Struct Biol , vol.174 , Issue.1 , pp. 84-91
    • Ryan, A.J.1    Ghuman, J.2    Zunszain, P.A.3    Chung, C.W.4    Curry, S.5
  • 3
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G, Birkett DJ, Wade DN, (1975) The characterization of two specific drug binding sites on human serum albumin. Mol Pharmacol 11: 824-832.
    • (1975) Mol Pharmacol , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 4
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • Sudlow G, Birkett DJ, Wade DN, (1976) Further characterization of specific drug binding sites on human serum albumin. Mol Pharmacol 12: 1052-1061.
    • (1976) Mol Pharmacol , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 5
    • 0020063750 scopus 로고
    • Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone
    • Fehske KJ, Schhtfer U, Wollert U, Mtiller WE, (1982) Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone. Mol Pharmacol 21(2): 387-393.
    • (1982) Mol Pharmacol , vol.21 , Issue.2 , pp. 387-393
    • Fehske, K.J.1    Schhtfer, U.2    Wollert, U.3    Mtiller, W.E.4
  • 9
    • 84883960468 scopus 로고    scopus 로고
    • Basic Pharmacokinetics and Pharmacodynamics: An Integrated Textbook and Computer Simulations
    • Rosenbaum SE (2011) Basic Pharmacokinetics and Pharmacodynamics: An Integrated Textbook and Computer Simulations. Wiley. 448 p.
    • (2011) Wiley , pp. 448
    • Rosenbaum, S.E.1
  • 10
    • 84875166973 scopus 로고    scopus 로고
    • Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking
    • Epub 2013 Mar 20
    • Zhang X, Li L, Xu Z, Liang Z, Su J, et al. (2013) Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking. PLoS One 8(3). Epub 2013 Mar 20.
    • (2013) PLoS One , vol.8 , Issue.3
    • Zhang, X.1    Li, L.2    Xu, Z.3    Liang, Z.4    Su, J.5
  • 11
    • 0031922522 scopus 로고    scopus 로고
    • Monoacylglycerol binding to human serum albumin: evidence that monooleoylglycerol binds at the dansylsarcosine site
    • Thumser AE, Buckland AG, Wilton DC, (1998) Monoacylglycerol binding to human serum albumin: evidence that monooleoylglycerol binds at the dansylsarcosine site. J Lipid Res 39(5): 1033-1038.
    • (1998) J Lipid Res , vol.39 , Issue.5 , pp. 1033-1038
    • Thumser, A.E.1    Buckland, A.G.2    Wilton, D.C.3
  • 12
    • 84872311586 scopus 로고    scopus 로고
    • Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies. J Biol Inorg Chem
    • Dömötör O, Hartinger CG, Bytzek AK, Kiss T, Keppler BK, et al. (2012) Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies. J Biol Inorg Chem. 18(1): 9-17.
    • (2012) , vol.18 , Issue.1 , pp. 9-17
    • Dömötör, O.1    Hartinger, C.G.2    Bytzek, A.K.3    Kiss, T.4    Keppler, B.K.5
  • 13
    • 79953041186 scopus 로고    scopus 로고
    • Site-dependent photo-fries rearrangement within serum albumins
    • Marin M, Lhiaubet-Vallet V, Miranda MA, (2011) Site-dependent photo-fries rearrangement within serum albumins. J Phys Chem B. 115(12): 2910-2915.
    • (2011) J Phys Chem B , vol.115 , Issue.12 , pp. 2910-2915
    • Marin, M.1    Lhiaubet-Vallet, V.2    Miranda, M.A.3
  • 14
    • 0028214507 scopus 로고
    • Binding sites of fluorescent probes on human serum albumin
    • Muller N, Lapicque F, Drelon E, Netter P, (1994) Binding sites of fluorescent probes on human serum albumin. J Pharm Pharmacol 46(4): 300-304.
    • (1994) J Pharm Pharmacol , vol.46 , Issue.4 , pp. 300-304
    • Muller, N.1    Lapicque, F.2    Drelon, E.3    Netter, P.4
  • 16
    • 77955551908 scopus 로고    scopus 로고
    • Study on the binding of chiral drug duloxetine hydrochloride to human serum albumin
    • Liu X, Du Y, (2010) Study on the binding of chiral drug duloxetine hydrochloride to human serum albumin. Eur J Med Chem 45(9): 4043-4049.
    • (2010) Eur J Med Chem , vol.45 , Issue.9 , pp. 4043-4049
    • Liu, X.1    Du, Y.2
  • 17
    • 39749188802 scopus 로고    scopus 로고
    • Species-dependent stereoselective drug binding to albumin: a circular dichroism study
    • Pistolozzi M, Bertucci C, (2008) Species-dependent stereoselective drug binding to albumin: a circular dichroism study. Chirality 20(3-4): 552-558.
    • (2008) Chirality , vol.20 , Issue.3-4 , pp. 552-558
    • Pistolozzi, M.1    Bertucci, C.2
  • 18
    • 0023743229 scopus 로고
    • Location and characterization of the warfarin binding site of human serum albumin. A comparative study of two large fragments
    • Bos OJ, Remijn JP, Fischer MJ, Wilting J, Janssen LH, (1988) Location and characterization of the warfarin binding site of human serum albumin. A comparative study of two large fragments. Biochem Pharmacol 37(20): 3905-3909.
    • (1988) Biochem Pharmacol , vol.37 , Issue.20 , pp. 3905-3909
    • Bos, O.J.1    Remijn, J.P.2    Fischer, M.J.3    Wilting, J.4    Janssen, L.H.5
  • 19
    • 61449110165 scopus 로고    scopus 로고
    • Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism
    • Nozaki A, Hori M, Kimura T, Ito H, Hatano T, (2009) Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism. Chem Pharm Bull (Tokyo) 57(2): 224-228.
    • (2009) Chem Pharm Bull (Tokyo) , vol.57 , Issue.2 , pp. 224-228
    • Nozaki, A.1    Hori, M.2    Kimura, T.3    Ito, H.4    Hatano, T.5
  • 20
    • 77951533737 scopus 로고    scopus 로고
    • Interactions between quercetin and warfarin for albumin binding: A new eye on food/drug interference
    • Di Bari L, Ripoli S, Pradhan S, Salvadori P, (2010) Interactions between quercetin and warfarin for albumin binding: A new eye on food/drug interference. Chirality 22(6): 593-596.
    • (2010) Chirality , vol.22 , Issue.6 , pp. 593-596
    • Di Bari, L.1    Ripoli, S.2    Pradhan, S.3    Salvadori, P.4
  • 21
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Ace CN, Vajdos F, Fee L, Grimsley G, Gray T, (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Ace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 22
    • 1542299070 scopus 로고    scopus 로고
    • Fluorescence quenching methods to study protein-nucleic acid interactions
    • Roy, S. Fluorescence quenching methods to study protein-nucleic acid interactions. Methods Enzymol. 2004, 379, 175-187.
    • (2004) Methods Enzymol , vol.379 , pp. 175-187
    • Roy, S.1
  • 24
    • 84864027393 scopus 로고    scopus 로고
    • Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation
    • Petrônio MS, Ximenes VF, (2012) Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation. Biochim Biophys Acta 1824(10): 1090-1096.
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.10 , pp. 1090-1096
    • Petrônio, M.S.1    Ximenes, V.F.2
  • 25
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process
    • Ware WR, (1962) Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J Phys Chem 66: 455-458.
    • (1962) J Phys Chem , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 26
    • 1542299070 scopus 로고    scopus 로고
    • Fluorescence quenching methods to study protein-nucleic acid interactions
    • Roy S, (2004) Fluorescence quenching methods to study protein-nucleic acid interactions. Methods Enzymol 379: 175-187.
    • (2004) Methods Enzymol , vol.379 , pp. 175-187
    • Roy, S.1
  • 27
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • Van de Weert M, Stella L, (2011) Fluorescence quenching and ligand binding: A critical discussion of a popular methodology. J Mol Struct 998(1-3): 144-150.
    • (2011) J Mol Struct , vol.998 , Issue.1-3 , pp. 144-150
    • van de Weert, M.1    Stella, L.2
  • 28
    • 17844410084 scopus 로고    scopus 로고
    • Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide
    • Sun C, Yang J, Wu X, Huang X, Wang F, et al. (2005) Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide. Biophys J 88(5): 3518-3524.
    • (2005) Biophys J , vol.88 , Issue.5 , pp. 3518-3524
    • Sun, C.1    Yang, J.2    Wu, X.3    Huang, X.4    Wang, F.5
  • 29
    • 39149126999 scopus 로고    scopus 로고
    • Probing the binding of morin to human serum albumin by optical spectroscopy
    • Qi ZD, Zhang Y, Liao FL, Ou-Yang YW, Liu Y, Yang X, (2008) Probing the binding of morin to human serum albumin by optical spectroscopy. J Pharm Biomed Anal 46(4): 699-706.
    • (2008) J Pharm Biomed Anal , vol.46 , Issue.4 , pp. 699-706
    • Qi, Z.D.1    Zhang, Y.2    Liao, F.L.3    Ou-Yang, Y.W.4    Liu, Y.5    Yang, X.6
  • 30
    • 38149074764 scopus 로고    scopus 로고
    • Spectroscopic studies on the binding of bromocresol purple to different serum albumins and its bilirubin displacing action
    • Faizul FM, Abdul Kadir H, Tayyab S, (2008) Spectroscopic studies on the binding of bromocresol purple to different serum albumins and its bilirubin displacing action. J Photochem Photobiol B 90(1): 1-7.
    • (2008) J Photochem Photobiol B , vol.90 , Issue.1 , pp. 1-7
    • Faizul, F.M.1    Abdul Kadir, H.2    Tayyab, S.3
  • 31
    • 79960207151 scopus 로고    scopus 로고
    • Spectroscopic and molecular modeling evidence of clozapine binding to human serum albumin at subdomain IIA
    • Wu X, Liu J, Wang Q, Xue W, Yao X, Zhang Y, Jin J, (2011) Spectroscopic and molecular modeling evidence of clozapine binding to human serum albumin at subdomain IIA. Spectrochim Acta A Mol Biomol Spectrosc 79(5): 1202-1209.
    • (2011) Spectrochim Acta A Mol Biomol Spectrosc , vol.79 , Issue.5 , pp. 1202-1209
    • Wu, X.1    Liu, J.2    Wang, Q.3    Xue, W.4    Yao, X.5    Zhang, Y.6    Jin, J.7
  • 32
    • 73449143528 scopus 로고    scopus 로고
    • Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease
    • Van der Veen BS, de Winther MP, Heeringa P, (2009) Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease. Antioxid Redox Signal 11: 2899-2937.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2899-2937
    • van der Veen, B.S.1    de Winther, M.P.2    Heeringa, P.3
  • 33
    • 79951945241 scopus 로고    scopus 로고
    • Taurine bromamine: a potent oxidant of tryptophan residues in albumin
    • Ximenes VF, da Fonseca LM, de Almeida AC, (2011) Taurine bromamine: a potent oxidant of tryptophan residues in albumin. Arch Biochem Biophys 507(2): 315-322.
    • (2011) Arch Biochem Biophys , vol.507 , Issue.2 , pp. 315-322
    • Ximenes, V.F.1    da Fonseca, L.M.2    de Almeida, A.C.3
  • 34
    • 84864027393 scopus 로고    scopus 로고
    • Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation
    • Petrônio MS, Ximenes VF, (2012) Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation. Biochim Biophys Acta 1824(10): 1090-1096.
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.10 , pp. 1090-1096
    • Petrônio, M.S.1    Ximenes, V.F.2
  • 36
    • 84885782454 scopus 로고    scopus 로고
    • Oxidation of Bovine Albumin by Hypochlorous and Hypobromous Acids: Structural and Functional Alterations
    • Petrônio MS, Fernandes JR, Menezes ML, Ximenes VF, (2013) Oxidation of Bovine Albumin by Hypochlorous and Hypobromous Acids: Structural and Functional Alterations. Br J Pharm Res 3(1): 147-160.
    • (2013) Br J Pharm Res , vol.3 , Issue.1 , pp. 147-160
    • Petrônio, M.S.1    Fernandes, J.R.2    Menezes, M.L.3    Ximenes, V.F.4
  • 38
    • 79952446257 scopus 로고    scopus 로고
    • Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin
    • Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S, (2011) Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol 174(1): 84-91.
    • (2011) J Struct Biol , vol.174 , Issue.1 , pp. 84-91
    • Ryan, A.J.1    Ghuman, J.2    Zunszain, P.A.3    Chung, C.W.4    Curry, S.5
  • 39
    • 84861371000 scopus 로고    scopus 로고
    • Interaction of virstatin with human serum albumin: spectroscopic analysis and molecular modeling
    • doi:10.1371/journal.pone.0037468
    • Chatterjee T, Pal A, Dey S, Chatterjee BK, Chakrabarti P, (2012) Interaction of virstatin with human serum albumin: spectroscopic analysis and molecular modeling. PLOS One 7(5): e37468 doi:10.1371/journal.pone.0037468.
    • (2012) PLOS One , vol.7 , Issue.5
    • Chatterjee, T.1    Pal, A.2    Dey, S.3    Chatterjee, B.K.4    Chakrabarti, P.5
  • 40
    • 0034602966 scopus 로고    scopus 로고
    • Conformational transitions of the three recombinant domains of human serum albumin depending on pH
    • Dockal M, Carter DC, Rüker F, (2000) Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J Biol Chem 275(5): 3042-3050.
    • (2000) J Biol Chem , vol.275 , Issue.5 , pp. 3042-3050
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3


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