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Volumn 90, Issue 2, 2008, Pages 126-134

The investigation of the interaction between 5-Iodouracil and human serum albumin by spectroscopic and modeling methods and determination of protein by synchronous fluorescence technique

Author keywords

5 Iodouracil; Binding constant; Determination; Energy transfer; Fluorescence; Human serum albumin (HSA); Interaction; Modeling; Quenching; Synchronous fluorescence

Indexed keywords


EID: 38149119814     PISSN: 00483575     EISSN: 10959939     Source Type: Journal    
DOI: 10.1016/j.pestbp.2007.11.002     Document Type: Article
Times cited : (49)

References (43)
  • 2
    • 0023354355 scopus 로고
    • Protein binding as a primary determinant of the clinical pharmacokinetic properties of non-steroidal anti-inflammatory drugs
    • Lin J.H., Cocchetto D.M., and Duggan D.E. Protein binding as a primary determinant of the clinical pharmacokinetic properties of non-steroidal anti-inflammatory drugs. Clin. Pharmacokinet. 12 (1987) 402-432
    • (1987) Clin. Pharmacokinet. , vol.12 , pp. 402-432
    • Lin, J.H.1    Cocchetto, D.M.2    Duggan, D.E.3
  • 3
    • 14744275227 scopus 로고    scopus 로고
    • High-throughput solution-based medicinal library screening against human serum albumin
    • Flarakos J., Morand K.L., and Vours P. High-throughput solution-based medicinal library screening against human serum albumin. Anal. Chem. 77 (2005) 1345-1353
    • (2005) Anal. Chem. , vol.77 , pp. 1345-1353
    • Flarakos, J.1    Morand, K.L.2    Vours, P.3
  • 4
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
    • Hu Y.J., Liu Y., Pi Z.B., and Qu S.S. Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study. Bioorg. Med. Chem. 13 (2005) 6609-6614
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6609-6614
    • Hu, Y.J.1    Liu, Y.2    Pi, Z.B.3    Qu, S.S.4
  • 5
    • 33646263355 scopus 로고    scopus 로고
    • Determination of proteins at nanogram levels with Bordeaux red based on the enhancement of resonance light scattering
    • Feng S.L., Pan Z.H., and Fan J. Determination of proteins at nanogram levels with Bordeaux red based on the enhancement of resonance light scattering. Spectrochimica Acta A 64 (2006) 574-579
    • (2006) Spectrochimica Acta A , vol.64 , pp. 574-579
    • Feng, S.L.1    Pan, Z.H.2    Fan, J.3
  • 6
    • 0034693453 scopus 로고    scopus 로고
    • Enzyme-catalyzed synthesis of sugar-containing monomers and linear polymers
    • Park O.J., Kim D.Y., and Dordick J.S. Enzyme-catalyzed synthesis of sugar-containing monomers and linear polymers. Biotechnol. Bioeng. 70 (2000) 208-216
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 208-216
    • Park, O.J.1    Kim, D.Y.2    Dordick, J.S.3
  • 7
    • 0034717010 scopus 로고    scopus 로고
    • Enzymatic peptide synthesis in organic solvent with different zeolites as immobilization matrixes
    • Guo W.X., Li X.W., Tian G.L., and Ye Y.H. Enzymatic peptide synthesis in organic solvent with different zeolites as immobilization matrixes. Tetrahedron 56 (2000) 3517-3522
    • (2000) Tetrahedron , vol.56 , pp. 3517-3522
    • Guo, W.X.1    Li, X.W.2    Tian, G.L.3    Ye, Y.H.4
  • 8
    • 38149007480 scopus 로고
    • Advances in hybrid antibiotic production research
    • Wang B.J., and Huang K. Advances in hybrid antibiotic production research. Chin. J. Pharm. 18 (1987) 378-382
    • (1987) Chin. J. Pharm. , vol.18 , pp. 378-382
    • Wang, B.J.1    Huang, K.2
  • 9
    • 9144221136 scopus 로고    scopus 로고
    • Binding of genistein to human serum albumin demonstrated using trytophan fluorescence quenching
    • Bian Q.Q., Liu J.Q., Tian J.N., and Hu Z.D. Binding of genistein to human serum albumin demonstrated using trytophan fluorescence quenching. Int. J. Biol. Macromol. 34 (2004) 275-279
    • (2004) Int. J. Biol. Macromol. , vol.34 , pp. 275-279
    • Bian, Q.Q.1    Liu, J.Q.2    Tian, J.N.3    Hu, Z.D.4
  • 10
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • Sulkowska A. Interaction of drugs with bovine and human serum albumin. J. Mol. Struct. 614 (2002) 227-232
    • (2002) J. Mol. Struct. , vol.614 , pp. 227-232
    • Sulkowska, A.1
  • 11
    • 33745249094 scopus 로고    scopus 로고
    • Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N′-(1-naphthyl) thiourea and serum albumin: Synchronous fluorescence determination of serum albumin
    • Cui F.L., Wang J.L., Cui Y.R., and Li J.P. Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N′-(1-naphthyl) thiourea and serum albumin: Synchronous fluorescence determination of serum albumin. Anal. Chim. Acta 571 (2006) 175-183
    • (2006) Anal. Chim. Acta , vol.571 , pp. 175-183
    • Cui, F.L.1    Wang, J.L.2    Cui, Y.R.3    Li, J.P.4
  • 12
    • 33847090590 scopus 로고
    • Prediction of peak wavelengths and intensities in synchronously excited fluorescence emission spectra
    • Lioyd J.B.F., and Evett I.W. Prediction of peak wavelengths and intensities in synchronously excited fluorescence emission spectra. Anal. Chem. 49 (1977) 1710-1715
    • (1977) Anal. Chem. , vol.49 , pp. 1710-1715
    • Lioyd, J.B.F.1    Evett, I.W.2
  • 13
    • 0036903551 scopus 로고    scopus 로고
    • Recent developments in multi-component synchronous fluorescence scan analysis TrAC
    • Patra D., and Mishra A.K. Recent developments in multi-component synchronous fluorescence scan analysis TrAC. Trends Anal. Chem. 21 (2002) 787-798
    • (2002) Trends Anal. Chem. , vol.21 , pp. 787-798
    • Patra, D.1    Mishra, A.K.2
  • 14
    • 2342509585 scopus 로고    scopus 로고
    • Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin
    • Liu J.Q., Tian J.N., He W.Y., Xie J.P., Hu Z.D., and Chen X.G. Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin. Pharm. Biomed. Anal. 35 (2004) 671-677
    • (2004) Pharm. Biomed. Anal. , vol.35 , pp. 671-677
    • Liu, J.Q.1    Tian, J.N.2    He, W.Y.3    Xie, J.P.4    Hu, Z.D.5    Chen, X.G.6
  • 15
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 16
    • 33745425770 scopus 로고    scopus 로고
    • Paracetamol and cytarabine binding competition in high affinity binding sites of transporting protein
    • Sulkowska A., Bojko B., Równicka J., and Sulkowski W.W. Paracetamol and cytarabine binding competition in high affinity binding sites of transporting protein. J. Mol. Struct. 792-793 (2006) 249-256
    • (2006) J. Mol. Struct. , vol.792-793 , pp. 249-256
    • Sulkowska, A.1    Bojko, B.2    Równicka, J.3    Sulkowski, W.W.4
  • 17
    • 0033103292 scopus 로고    scopus 로고
    • Studies on the interactions between human serum albumin and imidazolium [trans-tetrachlorobis (imidazol) ruthenate (III)]
    • Trynda-Lemiesz L., Keppler B.K., and Koztowski H. Studies on the interactions between human serum albumin and imidazolium [trans-tetrachlorobis (imidazol) ruthenate (III)]. J. Inorg. Biochem. 73 (1999) 123-128
    • (1999) J. Inorg. Biochem. , vol.73 , pp. 123-128
    • Trynda-Lemiesz, L.1    Keppler, B.K.2    Koztowski, H.3
  • 19
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen-probe for structural fluctuations in macromolecules
    • Lakowicz J.R., and Weber J.G. Quenching of fluorescence by oxygen-probe for structural fluctuations in macromolecules. Biochemistry 12 (1973) 4161-4170
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, J.G.2
  • 20
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution, an experimental study of the diffusion process
    • Ware W.R. Oxygen quenching of fluorescence in solution, an experimental study of the diffusion process. J. Phys. Chem. 66 (1962) 455-458
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 21
    • 0033907229 scopus 로고    scopus 로고
    • Measuring the forces that control protein interactions
    • Leckband D.A. Measuring the forces that control protein interactions. Rev. Biophys. Biomol. Struct. 29 (2000) 1-26
    • (2000) Rev. Biophys. Biomol. Struct. , vol.29 , pp. 1-26
    • Leckband, D.A.1
  • 22
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions-forced contributing to stability
    • Ross P.D., and Subramanian S. Thermodynamics of protein association reactions-forced contributing to stability. Biochemistry 20 (1981) 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 23
    • 33947553005 scopus 로고
    • The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in protein
    • Neméthy G., and Scheraga H.A. The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in protein. J. Phys. Chem. 66 (1962) 1773-1789
    • (1962) J. Phys. Chem. , vol.66 , pp. 1773-1789
    • Neméthy, G.1    Scheraga, H.A.2
  • 24
    • 0010714008 scopus 로고
    • Thermodynamic of protein interactions
    • Peeters H. (Ed), Pergamon Press, Oxford
    • Timasheff S.N. Thermodynamic of protein interactions. In: Peeters H. (Ed). Proteins of Biological Fluids (1972), Pergamon Press, Oxford
    • (1972) Proteins of Biological Fluids
    • Timasheff, S.N.1
  • 25
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. The attractions of proteins for small molecules and ions. Ann. NY Acad. Sci. 51 (1949) 660-672
    • (1949) Ann. NY Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 26
    • 7944227678 scopus 로고    scopus 로고
    • Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin
    • Hu Y.J., Liu Y., Wang J.B., Xiao X.H., and Qu S.S. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J. Pharm. Biochim. Anal. 36 (2004) 915-919
    • (2004) J. Pharm. Biochim. Anal. , vol.36 , pp. 915-919
    • Hu, Y.J.1    Liu, Y.2    Wang, J.B.3    Xiao, X.H.4    Qu, S.S.5
  • 27
    • 11344257292 scopus 로고    scopus 로고
    • Molecular spectroscopic study on the interaction of tetracyclines with serum albumins
    • Bi S.Y., Song D.Q., Tian Y., Zhou X., Liu Z.Y., and Zhang H.Q. Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochimca Acta A61 (2005) 629-636
    • (2005) Spectrochimca Acta , vol.A61 , pp. 629-636
    • Bi, S.Y.1    Song, D.Q.2    Tian, Y.3    Zhou, X.4    Liu, Z.Y.5    Zhang, H.Q.6
  • 30
    • 0003468776 scopus 로고    scopus 로고
    • Sinanoglu O. (Ed), Academic Press, New York
    • Förster T. In: Sinanoglu O. (Ed). Modern Quantum Chemistry vol. 3 (1996), Academic Press, New York
    • (1996) Modern Quantum Chemistry , vol.3
    • Förster, T.1
  • 32
    • 0015340490 scopus 로고
    • Proximity relationships in rhodopsin
    • Wu C.W., and Stryer L. Proximity relationships in rhodopsin. Proc. Natl. Acad. Sci. USA 69 (1972) 1104-1108
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1104-1108
    • Wu, C.W.1    Stryer, L.2
  • 34
    • 0346040439 scopus 로고    scopus 로고
    • Interaction between 1-benzoyl-4-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy
    • Cui F.L., Fan J., Li J.P., and Hu Z.D. Interaction between 1-benzoyl-4-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg. Med. Chem. 12 (2004) 151-157
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 151-157
    • Cui, F.L.1    Fan, J.2    Li, J.P.3    Hu, Z.D.4
  • 36
    • 0034963992 scopus 로고    scopus 로고
    • The subsequent effect of interaction between Co and human serum albumin or bovine serum albumin
    • Liang H., Huang J., Tu C.Q., Zhang M., Zhou Y.Q., and Shen P.W. The subsequent effect of interaction between Co and human serum albumin or bovine serum albumin. J. Inorg. Biochem. 85 (2001) 167-171
    • (2001) J. Inorg. Biochem. , vol.85 , pp. 167-171
    • Liang, H.1    Huang, J.2    Tu, C.Q.3    Zhang, M.4    Zhou, Y.Q.5    Shen, P.W.6
  • 38
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin
    • Petitpas I., Bhattacharya A.A., Twine S., East M., and Curry S. Crystal structure analysis of warfarin binding to human serum albumin. J. Biol. Chem. 276 (2001) 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
  • 39
    • 38149034021 scopus 로고    scopus 로고
    • SYBYL Software, Version 6.9.1, St. Louis, Tripos Associates Inc, 2003.
  • 40
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4*
    • Morris G.M., Goodsell D.S., Huey R., and Olson A.J. Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4*. J. Comput.-Aided Mol. Des. 10 (1996) 296-304
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , pp. 296-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 41
  • 42
    • 0037151702 scopus 로고    scopus 로고
    • Synchronous fluorescence determination of protein with functionalized CdS nanoparticles as a fluorescence probe
    • Wang L.Y., Zhou Y.Y., and Wang L. Synchronous fluorescence determination of protein with functionalized CdS nanoparticles as a fluorescence probe. Anal. Chim. Acta 466 (2002) 87-92
    • (2002) Anal. Chim. Acta , vol.466 , pp. 87-92
    • Wang, L.Y.1    Zhou, Y.Y.2    Wang, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.