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Volumn 6, Issue 11, 2011, Pages

Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics

Author keywords

[No Author keywords available]

Indexed keywords

1 NAPHTHOL; 2 NAPHTHOL; 8 QUINOLINOL; BILIRUBIN; DIAZEPAM; HEMIN; HUMAN SERUM ALBUMIN; IBUPROFEN; PHENYLBUTAZONE; WARFARIN; SERUM ALBUMIN;

EID: 80355136403     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026186     Document Type: Article
Times cited : (147)

References (49)
  • 1
    • 33644875222 scopus 로고    scopus 로고
    • Exposure to nonpersistent insecticides and male reproductive hormones
    • Meeker JD, Ryan L, Barr DB, Hauser R, (2006) Exposure to nonpersistent insecticides and male reproductive hormones. Epidemiology 17: 61-68.
    • (2006) Epidemiology , vol.17 , pp. 61-68
    • Meeker, J.D.1    Ryan, L.2    Barr, D.B.3    Hauser, R.4
  • 2
    • 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
  • 3
    • 0031104643 scopus 로고    scopus 로고
    • Construction and characterization of a manganese-binding site in cytochrome c peroxidase: towards a novel manganese peroxidase
    • Yeung BKS, Xiaotang W, Sigman JA, Petillo PA, Lu Y, (1997) Construction and characterization of a manganese-binding site in cytochrome c peroxidase: towards a novel manganese peroxidase. Chem Biol 4: 215-221.
    • (1997) Chem Biol , vol.4 , pp. 215-221
    • Yeung, B.K.S.1    Xiaotang, W.2    Sigman, J.A.3    Petillo, P.A.4    Lu, Y.5
  • 5
    • 0032495131 scopus 로고    scopus 로고
    • Investigation of the interaction between acridine orange and bovine serum albumin
    • Feng XZ, Lin Z, Yang LJ, Wang C, Bai CL, (1998) Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 47: 1223-1229.
    • (1998) Talanta , vol.47 , pp. 1223-1229
    • Feng, X.Z.1    Lin, Z.2    Yang, L.J.3    Wang, C.4    Bai, C.L.5
  • 6
    • 84981779372 scopus 로고
    • Intermolecular Energy Migration and Fluorescence
    • Förster T, (1948) Intermolecular Energy Migration and Fluorescence. Ann Phys 2: 55-75.
    • (1948) Ann Phys , vol.2 , pp. 55-75
    • Förster, T.1
  • 7
    • 0037123057 scopus 로고    scopus 로고
    • Interaction of Ochratoxin A with Human Serum Albumin. Preferential Binding of the Dianion and pH Effects
    • Il'ichev YV, Perry JL, Simon JD, (2002) Interaction of Ochratoxin A with Human Serum Albumin. Preferential Binding of the Dianion and pH Effects. J Phys Chem B 106: 452-459.
    • (2002) J Phys Chem B , vol.106 , pp. 452-459
    • Il'ichev, Y.V.1    Perry, J.L.2    Simon, J.D.3
  • 9
    • 43749115958 scopus 로고    scopus 로고
    • Isothermal titration calorimetric and spectroscopic studies on (alcohol+salt) induced partially folded state of a-lactalbumin and its binding with 8-anilino-1-naphthalenesulfonic acid
    • Sharma R, Kishore N, (2008) Isothermal titration calorimetric and spectroscopic studies on (alcohol+salt) induced partially folded state of a-lactalbumin and its binding with 8-anilino-1-naphthalenesulfonic acid. J Chem Thermodyn 2: 1141-1151.
    • (2008) J Chem Thermodyn , vol.2 , pp. 1141-1151
    • Sharma, R.1    Kishore, N.2
  • 10
    • 80355128480 scopus 로고
    • Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York
    • Bevington PR, (1969) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York.
    • (1969)
    • Bevington, P.R.1
  • 11
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov PL, Potekhin SA, (1987) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 131: 4-51.
    • (1987) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 12
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4 Automated docking with selective receptor flexibility
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, et al. (2009) AutoDock4 and AutoDockTools4 Automated docking with selective receptor flexibility. J Comput Chem 16: 2785-2791.
    • (2009) J Comput Chem , vol.16 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5
  • 13
    • 0036022960 scopus 로고    scopus 로고
    • Further Development and Validation of Empirical Scoring Functions for Structure-Based Binding Affinity Prediction
    • Wang R, Lai L, Wang S, (2002) Further Development and Validation of Empirical Scoring Functions for Structure-Based Binding Affinity Prediction. J Comput Aided Mol Des 16: 11-26.
    • (2002) J Comput Aided Mol Des , vol.16 , pp. 11-26
    • Wang, R.1    Lai, L.2    Wang, S.3
  • 14
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM, (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8: 127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 15
    • 80355124671 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, USA
    • DeLano WL, (2002) The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, USA.
    • (2002)
    • DeLano, W.L.1
  • 17
    • 80355134000 scopus 로고
    • NACCESS, Computer Program, Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard SJ, Thornton JM, (1993) NACCESS, Computer Program, Department of Biochemistry and Molecular Biology, University College, London.
    • (1993)
    • Hubbard, S.J.1    Thornton, J.M.2
  • 18
    • 37049030373 scopus 로고    scopus 로고
    • Investigating the binding of curcumin derivatives to bovine serum albumin
    • Sahoo BK, Ghosh KS, Dasgupta S, (2008) Investigating the binding of curcumin derivatives to bovine serum albumin. Biophys Chem 132: 81-88.
    • (2008) Biophys Chem , vol.132 , pp. 81-88
    • Sahoo, B.K.1    Ghosh, K.S.2    Dasgupta, S.3
  • 19
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP, Freire E, (1992) Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 43: 313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 20
    • 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
  • 21
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
    • Flora K, Brennan JD, Baker GA, Doody MA, Bright FV, (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys J 75: 1084-1096.
    • (1998) Biophys J , vol.75 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 22
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross PD, Subramanian S, (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20: 3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 23
    • 23444447825 scopus 로고    scopus 로고
    • Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method
    • Hu YJ, Liu Y, Zhang LX, (2005) Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. J Mol Struct 750: 174-178.
    • (2005) J Mol Struct , vol.750 , pp. 174-178
    • Hu, Y.J.1    Liu, Y.2    Zhang, L.X.3
  • 24
    • 11344257292 scopus 로고    scopus 로고
    • Molecular Spectroscopic Study on the Interaction of Tetracyclines with Serum Albumins
    • Bi SY, Song DQ, Tian Y, Zhou X, Liu Z, et al. (2005) Molecular Spectroscopic Study on the Interaction of Tetracyclines with Serum Albumins. Spectrochim Acta A 61: 629-636.
    • (2005) Spectrochim Acta A , vol.61 , pp. 629-636
    • Bi, S.Y.1    Song, D.Q.2    Tian, Y.3    Zhou, X.4    Liu, Z.5
  • 26
    • 0032867556 scopus 로고    scopus 로고
    • The three recombinant domains of human serum albumin. Structural characterization and ligand binding properties
    • Dockal M, Carter DC, Rüker F, (1999) The three recombinant domains of human serum albumin. Structural characterization and ligand binding properties. J Biol Chem 274: 29303-29310.
    • (1999) J Biol Chem , vol.274 , pp. 29303-29310
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3
  • 28
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I
    • Petitpas I, Bhattacharya AA, Twine S, East M, Curry S, (2001) Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J Biol Chem 276: 22804-22809.
    • (2001) J Biol Chem , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 30
    • 0022387828 scopus 로고
    • Evidence for the fatty acid-induced heterogeneity of the N and B conformations of human serum albumin
    • Dröge JH, Janssen LH, Wilting J, (1985) Evidence for the fatty acid-induced heterogeneity of the N and B conformations of human serum albumin. Biochem Pharmacol 34: 3299-3304.
    • (1985) Biochem Pharmacol , vol.34 , pp. 3299-3304
    • Dröge, J.H.1    Janssen, L.H.2    Wilting, J.3
  • 31
    • 0036305832 scopus 로고    scopus 로고
    • Artificial Protein Cavities as Specific Ligand-binding Templates: Characterization of an Engineered Heterocyclic Cation-binding Site that Preserves the Evolved Specificity of the Parent Protein
    • Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, (2002) Artificial Protein Cavities as Specific Ligand-binding Templates: Characterization of an Engineered Heterocyclic Cation-binding Site that Preserves the Evolved Specificity of the Parent Protein. J Mol Biol 315: 845-857.
    • (2002) J Mol Biol , vol.315 , pp. 845-857
    • Musah, R.A.1    Jensen, G.M.2    Bunte, S.W.3    Rosenfeld, R.J.4    Goodin, D.B.5
  • 32
    • 0344304434 scopus 로고    scopus 로고
    • The tandem Src homology 2 domain of the Syk kinase: a molecular device that adapts to interphosphotyrosine distances
    • Kumaran S, Grucza RA, Waksman G, (2003) The tandem Src homology 2 domain of the Syk kinase: a molecular device that adapts to interphosphotyrosine distances. Proc Natl Acad Sci U S A 100: 14828-14833.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14828-14833
    • Kumaran, S.1    Grucza, R.A.2    Waksman, G.3
  • 34
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record MT, (1994) Coupling of local folding to site-specific binding of proteins to DNA. Science 263: 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 35
    • 0014690424 scopus 로고
    • Changes in ultraviolet absorption produced by alteration of protein conformation
    • Donovan JW, (1969) Changes in ultraviolet absorption produced by alteration of protein conformation. J Biol Chem 244: 1961-1967.
    • (1969) J Biol Chem , vol.244 , pp. 1961-1967
    • Donovan, J.W.1
  • 36
    • 52649154595 scopus 로고    scopus 로고
    • Gold Nanorods as Nanoadmicelles: 1-Naphthol Partitioning into a Nanorod-Bound Surfactant Bilayer
    • Alkilany AM, Frey RL, Ferry JL, Murphy CJ, (2008) Gold Nanorods as Nanoadmicelles: 1-Naphthol Partitioning into a Nanorod-Bound Surfactant Bilayer. Langmuir 24: 10235-10239.
    • (2008) Langmuir , vol.24 , pp. 10235-10239
    • Alkilany, A.M.1    Frey, R.L.2    Ferry, J.L.3    Murphy, C.J.4
  • 37
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Kragh-Hansen U, (1990) Structure and ligand binding properties of human serum albumin. Dan Med Bull 37: 57-84.
    • (1990) Dan Med Bull , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 38
    • 80355139905 scopus 로고    scopus 로고
    • Laboratory write up from Physical Chemistry Laboratory, Department of Chemistry, Vassar College
    • Gomez MA, (2003) Excited State Properties of 2-Naphthol. Laboratory write up from Physical Chemistry Laboratory, Department of Chemistry, Vassar College.
    • (2003) Excited State Properties of 2-Naphthol
    • Gomez, M.A.1
  • 39
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov I, Bosshard HR, (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 12: 3-18.
    • (1999) J Mol Recognit , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 40
    • 76949101961 scopus 로고    scopus 로고
    • Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy
    • Otosu T, Nishimoto E, Yamashita S, (2010) Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy. J Biochem 147: 191-200.
    • (2010) J Biochem , vol.147 , pp. 191-200
    • Otosu, T.1    Nishimoto, E.2    Yamashita, S.3
  • 41
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures
    • Bhattacharya AA, Curry S, Franks NP, (2000) Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem 275: 38731-38738.
    • (2000) J Biol Chem , vol.275 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 42
    • 0022780017 scopus 로고
    • Influence of inhibitor binding on the internal motions of lysozyme
    • Cross AJ, Fleming GR, (1986) Influence of inhibitor binding on the internal motions of lysozyme. Biophys J 50: 507-512.
    • (1986) Biophys J , vol.50 , pp. 507-512
    • Cross, A.J.1    Fleming, G.R.2
  • 43
    • 0029952364 scopus 로고    scopus 로고
    • A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity
    • Fitzgerald MM, Musah RA, McRee DE, Goodin DB, (1996) A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity. Nat Struct Biol 3: 626-631.
    • (1996) Nat Struct Biol , vol.3 , pp. 626-631
    • Fitzgerald, M.M.1    Musah, R.A.2    McRee, D.E.3    Goodin, D.B.4
  • 44
    • 33745454971 scopus 로고    scopus 로고
    • Thermodynamic Insights into the Binding of Triton X-100 to Globular Proteins: A Calorimetric and Spectroscopic Investigation
    • Singh SK, Kishore N, (2006) Thermodynamic Insights into the Binding of Triton X-100 to Globular Proteins: A Calorimetric and Spectroscopic Investigation. J Phys Chem B 110: 9728-9737.
    • (2006) J Phys Chem B , vol.110 , pp. 9728-9737
    • Singh, S.K.1    Kishore, N.2
  • 45
    • 52649127984 scopus 로고    scopus 로고
    • A survey of the year 2007 literature on applications of isothermal titration calorimetry
    • Bjelic S, Jelesarov I, (2008) A survey of the year 2007 literature on applications of isothermal titration calorimetry. J Mol Recognit 21: 289-311.
    • (2008) J Mol Recognit , vol.21 , pp. 289-311
    • Bjelic, S.1    Jelesarov, I.2
  • 46
    • 0019073710 scopus 로고
    • Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin
    • Adams PA, Berman MC, (1980) Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin. Biochem J 191: 95-102.
    • (1980) Biochem J , vol.191 , pp. 95-102
    • Adams, P.A.1    Berman, M.C.2
  • 47
    • 0002547347 scopus 로고
    • Physical chemistry of bilirubin: binding to macromolecules and membranes
    • In: Heirwegh KPM, Brown SB, editors, CRC Press, Boca Raton, FL
    • Brodersen R, (1982) Physical chemistry of bilirubin: binding to macromolecules and membranes. In: Heirwegh KPM, Brown SB, editors. Bilirubin, Vol. 1: Chemistry, CRC Press, Boca Raton, FL.
    • (1982) Bilirubin, Vol. 1: Chemistry
    • Brodersen, R.1
  • 48
    • 0025049741 scopus 로고
    • Determination of warfarin-human serum albumin protein binding parameters be an improved Hummel- Dreyer high performance liquid chromatographic method using internal surface reversed phase columns
    • Pinkerton TC, Koeplinger KA, (1990) Determination of warfarin-human serum albumin protein binding parameters be an improved Hummel- Dreyer high performance liquid chromatographic method using internal surface reversed phase columns. Anal Chem 62: 2114-2122.
    • (1990) Anal Chem , vol.62 , pp. 2114-2122
    • Pinkerton, T.C.1    Koeplinger, K.A.2
  • 49
    • 0026021941 scopus 로고
    • Octanoate binding to the indole and benzodiazepine binding region of human serum albumin
    • Kragh-Hansen U, (1991) Octanoate binding to the indole and benzodiazepine binding region of human serum albumin. Biochem J 273: 641-644.
    • (1991) Biochem J , vol.273 , pp. 641-644
    • Kragh-Hansen, U.1


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