메뉴 건너뛰기




Volumn 9, Issue 1, 2010, Pages 93-102

Photophysics and photochemistry of dyes bound to human serum albumin are determined by the dye localization

Author keywords

[No Author keywords available]

Indexed keywords


EID: 74049111204     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b9pp00091g     Document Type: Article
Times cited : (62)

References (58)
  • 1
    • 0021111937 scopus 로고
    • Singlet oxygen production by lactoperoxidase
    • J. R. Kanofsky Singlet oxygen production by lactoperoxidase J. Biol. Chem. 1983 258 10 5991 5993
    • (1983) J. Biol. Chem. , vol.258 , Issue.10 , pp. 5991-5993
    • Kanofsky, J.R.1
  • 2
    • 0021750194 scopus 로고
    • Biochemical requirements for singlet oxygen production by purified human myeloperoxidase
    • J. R. Kanofsky J. Wright G. E. Miles-Richardson A. I. Tauber Biochemical requirements for singlet oxygen production by purified human myeloperoxidase J. Clin. Invest. 1984 74 4 1489 1495
    • (1984) J. Clin. Invest. , vol.74 , Issue.4 , pp. 1489-1495
    • Kanofsky, J.R.1    Wright, J.2    Miles-Richardson, G.E.3    Tauber, A.I.4
  • 3
    • 0021352686 scopus 로고
    • Singlet oxygen production by chloroperoxidase-hydrogen peroxide-halide systems
    • J. R. Kanofsky Singlet oxygen production by chloroperoxidase-hydrogen peroxide-halide systems J. Biol. Chem. 1984 259 9 5596 5600
    • (1984) J. Biol. Chem. , vol.259 , Issue.9 , pp. 5596-5600
    • Kanofsky, J.R.1
  • 4
    • 0027185676 scopus 로고
    • Extra cellular production of singlet oxygen by stimulated macrophages quantified using 9,10-diphenylanthracene and beryline in a polystyrene film
    • M. J. Steinbeck A. U. Khan M. J. Kanjorski Extra cellular production of singlet oxygen by stimulated macrophages quantified using 9,10- diphenylanthracene and beryline in a polystyrene film J. Biol. Chem. 1993 268 15649 15654
    • (1993) J. Biol. Chem. , vol.268 , pp. 15649-15654
    • Steinbeck, M.J.1    Khan, A.U.2    Kanjorski, M.J.3
  • 7
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • M. J. Davies Singlet oxygen-mediated damage to proteins and its consequences Biochem. Biophys. Res. Commun. 2003 305 3 761 770
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , Issue.3 , pp. 761-770
    • Davies, M.J.1
  • 8
    • 0036632772 scopus 로고    scopus 로고
    • Singlet oxygen-mediated protein oxidation: Evidence for the formation of reactive side chain peroxides on tyrosine residues
    • A. Wright W. A. Bubb C. L. Hawkins M. J. Davies Singlet oxygen-mediated protein oxidation: evidence for the formation of reactive side chain peroxides on tyrosine residues Photochem. Photobiol. 2002 76 1 35 46
    • (2002) Photochem. Photobiol. , vol.76 , Issue.1 , pp. 35-46
    • Wright, A.1    Bubb, W.A.2    Hawkins, C.L.3    Davies, M.J.4
  • 9
    • 85047695047 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack
    • P. E. Morgan R. T. Dean M. J. Davies Inhibition of glyceraldehyde-3- phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack Eur. J. Biochem. 2002 269 7 1916 1925
    • (2002) Eur. J. Biochem. , vol.269 , Issue.7 , pp. 1916-1925
    • Morgan, P.E.1    Dean, R.T.2    Davies, M.J.3
  • 10
    • 34247127332 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatases by amino acid, peptide, and protein hydroperoxides: Potential modulation of cell signaling by protein oxidation products
    • M. Gracanin M. J. Davies Inhibition of protein tyrosine phosphatases by amino acid, peptide, and protein hydroperoxides: potential modulation of cell signaling by protein oxidation products Free Radical Biol. Med. 2007 42 10 1543 1551
    • (2007) Free Radical Biol. Med. , vol.42 , Issue.10 , pp. 1543-1551
    • Gracanin, M.1    Davies, M.J.2
  • 11
    • 1242298607 scopus 로고    scopus 로고
    • Protective mechanisms against peptide and protein peroxides generated by singlet oxygen
    • P. E. Morgan R. T. Dean M. J. Davies Protective mechanisms against peptide and protein peroxides generated by singlet oxygen Free Radical Biol. Med. 2004 36 4 484 496
    • (2004) Free Radical Biol. Med. , vol.36 , Issue.4 , pp. 484-496
    • Morgan, P.E.1    Dean, R.T.2    Davies, M.J.3
  • 12
    • 0037443717 scopus 로고    scopus 로고
    • Photo-oxidation of cells generates long-lived intracellular protein peroxides
    • A. Wright C. L. Hawkins M. J. Davies Photo-oxidation of cells generates long-lived intracellular protein peroxides Free Radical Biol. Med. 2003 34 6 637 647
    • (2003) Free Radical Biol. Med. , vol.34 , Issue.6 , pp. 637-647
    • Wright, A.1    Hawkins, C.L.2    Davies, M.J.3
  • 13
    • 0034696781 scopus 로고    scopus 로고
    • Protein degradation by peroxide catalyzed by chromium (III): Role of coordinated ligand
    • H. Y. Shrivastava U. N. Balachandran Protein degradation by peroxide catalyzed by chromium (III): Role of coordinated ligand Biochem. Biophys. Res. Commun. 2000 270 3 749 754
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , Issue.3 , pp. 749-754
    • Shrivastava, H.Y.1    Balachandran, U.N.2
  • 14
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • E. R. Stadtman B. S. Berlett Reactive oxygen-mediated protein oxidation in aging and disease Chem. Res. Toxicol. 1997 10 5 485 494
    • (1997) Chem. Res. Toxicol. , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 15
    • 0022393446 scopus 로고
    • Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron
    • K. Kim S. G. Rhee E. R. Stadtman Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron J. Biol. Chem. 1985 260 29 15394 15397
    • (1985) J. Biol. Chem. , vol.260 , Issue.29 , pp. 15394-15397
    • Kim, K.1    Rhee, S.G.2    Stadtman, E.R.3
  • 16
    • 0033937772 scopus 로고    scopus 로고
    • Photosensitized production of singlet oxygen
    • I. E. Kochevar R. W. Redmond Photosensitized production of singlet oxygen Methods Enzymol. 2000 319 20 28
    • (2000) Methods Enzymol. , vol.319 , pp. 20-28
    • Kochevar, I.E.1    Redmond, R.W.2
  • 17
    • 0038266111 scopus 로고    scopus 로고
    • Influence of negatively charged interfaces on the ground and excited state properties of Methylene Blue
    • D. Severino H. C. Junqueira M. Gugliotti D. S. Gabrielli M. S. Baptista Influence of negatively charged interfaces on the ground and excited state properties of Methylene Blue Photochem. Photobiol. 2003 77 5 459 468
    • (2003) Photochem. Photobiol. , vol.77 , Issue.5 , pp. 459-468
    • Severino, D.1    Junqueira, H.C.2    Gugliotti, M.3    Gabrielli, D.S.4    Baptista, M.S.5
  • 18
    • 1942435295 scopus 로고    scopus 로고
    • Binding, aggregation and photochemical properties of methylene blue in mitochondrial suspensions
    • D. Gabrielli E. Belisle D. Severino A. J. Kowaltowski M. S. Baptista Binding, aggregation and photochemical properties of methylene blue in mitochondrial suspensions Photochem. Photobiol. 2004 79 3 227 232
    • (2004) Photochem. Photobiol. , vol.79 , Issue.3 , pp. 227-232
    • Gabrielli, D.1    Belisle, E.2    Severino, D.3    Kowaltowski, A.J.4    Baptista, M.S.5
  • 19
    • 0033212315 scopus 로고    scopus 로고
    • Effect of Self-association and Protein Binding on the Photochemical Reactivity of Triarylmethanes. Implications of Noncovalent Interactions on the Competition between Photosensitization Mechanisms Type i and Type II
    • J. A. Bartlett G. L. Indig Effect of Self-association and Protein Binding on the Photochemical Reactivity of Triarylmethanes. Implications of Noncovalent Interactions on the Competition between Photosensitization Mechanisms Type I and Type II Photochem. Photobiol. 1999 70 4 490 498
    • (1999) Photochem. Photobiol. , vol.70 , Issue.4 , pp. 490-498
    • Bartlett, J.A.1    Indig, G.L.2
  • 22
    • 14544267132 scopus 로고    scopus 로고
    • Binding of hypocrellin B to human serum albumin and photo-induced interactions
    • B. Zhao J. Xie J. Zhao Binding of hypocrellin B to human serum albumin and photo-induced interactions Biochim. Biophys. Acta, Gen. Subj. 2005 1722 2 124 130
    • (2005) Biochim. Biophys. Acta, Gen. Subj. , vol.1722 , Issue.2 , pp. 124-130
    • Zhao, B.1    Xie, J.2    Zhao, J.3
  • 23
    • 33745499607 scopus 로고    scopus 로고
    • The influence of human serum albumin on the photogeneration of singlet oxygen by meso-tetra(4-sulfonatophenyl)porphyrin. An infrared phosphorescence study
    • M. Korínek R. Dedic A. Molnár J. Hála The influence of human serum albumin on the photogeneration of singlet oxygen by meso-tetra(4-sulfonatophenyl)porphyrin. An infrared phosphorescence study J. Fluoresc. 2006 16 3 355 359
    • (2006) J. Fluoresc. , vol.16 , Issue.3 , pp. 355-359
    • Korínek, M.1    Dedic, R.2    Molnár, A.3    Hála, J.4
  • 24
    • 33745871186 scopus 로고    scopus 로고
    • Influence of Human Serum Albumin on Photodegradation of Folic Acid in Solution
    • P. Vorobey A. E. Steindal M. K. Off A. Vorobey J. Moan Influence of Human Serum Albumin on Photodegradation of Folic Acid in Solution Photochem. Photobiol. 2006 82 3 817 822
    • (2006) Photochem. Photobiol. , vol.82 , Issue.3 , pp. 817-822
    • Vorobey, P.1    Steindal, A.E.2    Off, M.K.3    Vorobey, A.4    Moan, J.5
  • 25
    • 0142094029 scopus 로고    scopus 로고
    • Porphyrin-induced photooxidation of conjugated bilirubin
    • N. Shishido K. Nakayama M. Nakamura Porphyrin-induced photooxidation of conjugated bilirubin Free Radical Res. 2003 37 10 1061 1067
    • (2003) Free Radical Res. , vol.37 , Issue.10 , pp. 1061-1067
    • Shishido, N.1    Nakayama, K.2    Nakamura, M.3
  • 26
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin (Review)
    • U. Kragh-Hansen Structure and ligand binding properties of human serum albumin (Review) Dan. Med. Bull. 1990 37 1 57 84
    • (1990) Dan. Med. Bull. , vol.37 , Issue.1 , pp. 57-84
    • Kragh-Hansen, U.1
  • 27
    • 0027408611 scopus 로고
    • Quantitative analyses of the interaction between calcium ions and human serum albumin
    • U. Kragh-Hansen Quantitative analyses of the interaction between calcium ions and human serum albumin Clin. Chem. 1993 39 2 202 208
    • (1993) Clin. Chem. , vol.39 , Issue.2 , pp. 202-208
    • Kragh-Hansen, U.1
  • 28
    • 0025322080 scopus 로고
    • Conformational changes in human serum albumin induced by ligand binding
    • B. Honore Conformational changes in human serum albumin induced by ligand binding Phamacol. Toxicol. 1990 66 2 7 26
    • (1990) Phamacol. Toxicol. , vol.66 , Issue.2 , pp. 7-26
    • Honore, B.1
  • 29
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X. M. He D. C. Carter Atomic structure and chemistry of human serum albumin Nature 1992 358 6383 209 215
    • (1992) Nature , vol.358 , Issue.6383 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 30
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow D. J. Birkett D. N. Wade The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 1975 11 6 824 832
    • (1975) Mol. Pharmacol. , vol.11 , Issue.6 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 31
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • G. Sudlow D. J. Birkett D. N. Wade Further characterization of specific drug binding sites on human serum albumin Mol. Pharmacol. 1976 12 6 1052 1061
    • (1976) Mol. Pharmacol. , vol.12 , Issue.6 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 32
    • 0033842504 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin-Tools for the characterization of the warfarin binding site
    • M. Dockal M. Chang D. C. Carter F. Ruker Five recombinant fragments of human serum albumin-Tools for the characterization of the warfarin binding site Protein Sci. 2000 9 8 1455 1465
    • (2000) Protein Sci. , vol.9 , Issue.8 , pp. 1455-1465
    • Dockal, M.1    Chang, M.2    Carter, D.C.3    Ruker, F.4
  • 36
    • 23944432680 scopus 로고    scopus 로고
    • Fluorometric investigation of the interaction between methylene blue and human serum albumin
    • Y.-J. Hu W. Lia Y. Liua J.-X. Donga S.-S. Qua Fluorometric investigation of the interaction between methylene blue and human serum albumin J. Pharm. Biomed. Anal. 2005 39 3-4 740 745
    • (2005) J. Pharm. Biomed. Anal. , vol.39 , Issue.34 , pp. 740-745
    • Hu, Y.-J.1    Lia, W.2    Liua, Y.3    Donga, J.-X.4    Qua, S.-S.5
  • 37
    • 4644291448 scopus 로고    scopus 로고
    • Flexibility in proteins: Tuning the sensitivity to O2 diffusion by varying the lifetime of a phosphorescent sensor in horseradish peroxidase
    • J. Nibbs S. A. Vinogradov J. M. Vanderkooi B. Zelent Flexibility in proteins: tuning the sensitivity to O2 diffusion by varying the lifetime of a phosphorescent sensor in horseradish peroxidase Photochem. Photobiol. 2004 80 1 36 40
    • (2004) Photochem. Photobiol. , vol.80 , Issue.1 , pp. 36-40
    • Nibbs, J.1    Vinogradov, S.A.2    Vanderkooi, J.M.3    Zelent, B.4
  • 39
    • 0025876389 scopus 로고
    • Intrinsic tryptophan phosphorescence as a marker of conformation and oxygen diffusion in purified cytochrome oxidase
    • S. Papp T. E. King J. M. Vanderkooi Intrinsic tryptophan phosphorescence as a marker of conformation and oxygen diffusion in purified cytochrome oxidase FEBS Lett. 1991 283 1 113 116
    • (1991) FEBS Lett. , vol.283 , Issue.1 , pp. 113-116
    • Papp, S.1    King, T.E.2    Vanderkooi, J.M.3
  • 40
    • 37049080392 scopus 로고
    • Experimental correction for the inner-filter effect in fluorescence spectra
    • M. Kubista R. Sojback S. Ericksson B. Albinsson Experimental correction for the inner-filter effect in fluorescence spectra Analyst 1994 119 3 417 419
    • (1994) Analyst , vol.119 , Issue.3 , pp. 417-419
    • Kubista, M.1    Sojback, R.2    Ericksson, S.3    Albinsson, B.4
  • 41
    • 0021353799 scopus 로고
    • Albumin binding of anti-inflammatory drugs. Utility of a site oriented versus a stoichiometric analysis
    • B. Honore R. Brodersen Albumin binding of anti-inflammatory drugs. Utility of a site oriented versus a stoichiometric analysis Mol. Pharmacol. 1984 25 1 137 150
    • (1984) Mol. Pharmacol. , vol.25 , Issue.1 , pp. 137-150
    • Honore, B.1    Brodersen, R.2
  • 42
    • 0025049741 scopus 로고
    • Determination of warfarin-human serum albumin protein binding parameters by an improved Hummel-Dreyer high-performance liquid chromatographic method using internal surface reversed-phase columns
    • T. C. Pinkerton K. A. Koeplinger Determination of warfarin-human serum albumin protein binding parameters by an improved Hummel-Dreyer high-performance liquid chromatographic method using internal surface reversed-phase columns Anal. Chem. 1990 62 19 2114 2122
    • (1990) Anal. Chem. , vol.62 , Issue.19 , pp. 2114-2122
    • Pinkerton, T.C.1    Koeplinger, K.A.2
  • 44
    • 33750513038 scopus 로고    scopus 로고
    • Automatic and highly reproducible RESP and ESP charge derivation: Application to the development of programs RED and X RED
    • California
    • A. Pigache, P. Cieplak and F. Y. Dupradeau, in Automatic and highly reproducible RESP and ESP charge derivation: Application to the development of programs RED and X RED, 227th ACS National Meeting, California, 2004, California, 2004
    • (2004) 227th ACS National Meeting, California
    • Pigache, A.1    Cieplak, P.2    Dupradeau, F.Y.3
  • 45
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • G. M. Morris D. S. Goodsell R. S. Halliday R. Huey W. E. Hart R. K. Belew A. J. Olson Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 1998 19 14 1639 1662
    • (1998) J. Comput. Chem. , vol.19 , Issue.14 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 46
    • 25844447139 scopus 로고    scopus 로고
    • Detergent binding as a sensor of hydrophobicity and polar interactions in the binding cavities of proteins
    • V. Peyre V. Lair V. André G. le Maire U. Kragh-Hansen M. le Maire J. V. Møller Detergent binding as a sensor of hydrophobicity and polar interactions in the binding cavities of proteins Langmuir 2005 21 19 8865 8875
    • (2005) Langmuir , vol.21 , Issue.19 , pp. 8865-8875
    • Peyre, V.1    Lair, V.2    André, V.3    Le Maire, G.4    Kragh-Hansen, U.5    Le Maire, M.6    Møller, J.V.7
  • 48
    • 0014210820 scopus 로고
    • Fluorescence Decay Times: Proteins, Coenzymes, and Other Compounds in Water
    • F. C. Raymond G. V. Gerald N. Alexander Fluorescence Decay Times: Proteins, Coenzymes, and Other Compounds in Water Science 1967 156 3777 949 951
    • (1967) Science , vol.156 , Issue.3777 , pp. 949-951
    • Raymond, F.C.1    Gerald, G.V.2    Alexander, N.3
  • 49
    • 21744445084 scopus 로고    scopus 로고
    • A molecular dynamics study of human serum albumin binding sites
    • R. Artali G. Bombieri L. Calabi A. Del Pra A molecular dynamics study of human serum albumin binding sites Farmaco 2005 60 6 7
    • (2005) Farmaco , vol.60 , pp. 6-7
    • Artali, R.1    Bombieri, G.2    Calabi, L.3    Del Pra, A.4
  • 52
    • 61449132323 scopus 로고    scopus 로고
    • Characterization of the mangiferin-human serum albumin complex by spectroscopic and molecular modeling approaches
    • Y. Yue X. Chen J. Qin X. Yao Characterization of the mangiferin-human serum albumin complex by spectroscopic and molecular modeling approaches J. Pharm. Biomed. Anal. 2009 49 3 753 759
    • (2009) J. Pharm. Biomed. Anal. , vol.49 , Issue.3 , pp. 753-759
    • Yue, Y.1    Chen, X.2    Qin, J.3    Yao, X.4
  • 53
    • 44149108388 scopus 로고    scopus 로고
    • Studies on the interaction of gallic acid with human serum albumin in membrane mimetic environments
    • Y. Zhang L. Dong J. Li X. Chen Studies on the interaction of gallic acid with human serum albumin in membrane mimetic environments Talanta 2008 76 2 246 253
    • (2008) Talanta , vol.76 , Issue.2 , pp. 246-253
    • Zhang, Y.1    Dong, L.2    Li, J.3    Chen, X.4
  • 54
    • 6344282904 scopus 로고    scopus 로고
    • Reactivity of Bovine Whey proteins, Peptides, and amino acids toward Triplet Riboflavin as studied by laser flash photolysis
    • D. R. Cardoso D. W. Franco K. Olsen M. L. Andersen L. F. Skibsted Reactivity of Bovine Whey Proteins, Peptides, and Amino Acids toward Triplet Riboflavin as Studied by Laser Flash Photolysis J. Agric. Food Chem. 2004 52 21 6602 6606
    • (2004) J. Agric. Food Chem. , vol.52 , Issue.21 , pp. 6602-6606
    • Cardoso, D.R.1    Franco, D.W.2    Olsen, K.3    Andersen, M.L.4    Skibsted, L.F.5
  • 55
    • 0015241501 scopus 로고
    • Differences between Bovine and Human Serum albumins: Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence fffects
    • J. Steinhardt J. Krijn J. G. Leidy Differences between Bovine and Human Serum albumins: Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence fffects Biochemistry 1971 10 22 4005 4015
    • (1971) Biochemistry , vol.10 , Issue.22 , pp. 4005-4015
    • Steinhardt, J.1    Krijn, J.2    Leidy, J.G.3
  • 57
    • 0033924511 scopus 로고    scopus 로고
    • Time-resolved singlet oxygen detection
    • S. Nonell S. E. Braslavsky Time-Resolved Singlet Oxygen Detection Methods Enzymol. 2000 319 37 49
    • (2000) Methods Enzymol. , vol.319 , pp. 37-49
    • Nonell, S.1    Braslavsky, S.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.