메뉴 건너뛰기




Volumn 86, Issue 3, 2010, Pages 538-544

Probing the binding interaction of a phenazinium dye with serum transport proteins: A combined fluorometric and circular dichroism study

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; COLORING AGENT; PHENAZINE DERIVATIVE; PHENOSAFRANINE; PLASMA PROTEIN; PROTEIN BINDING;

EID: 77951804336     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2009.00688.x     Document Type: Article
Times cited : (48)

References (42)
  • 2
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C. J. X. Ho (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153 176.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-176
    • Carter, D.C.1    Ho, J.X.2
  • 3
    • 41549131838 scopus 로고    scopus 로고
    • Transient absorption spectroscopy for determining multiple site occupancy in drug - Protein conjugates. A comparison between human and bovine serum albumins using flurbiprofen methyl ester as a probe
    • DOI 10.1021/jp076960q
    • Vaya, I., M. C. Jimenez M. A. Miranda (2008) Transient absorption spectroscopy for determining multiple site occupancy in drug-protein conjugates. A comparison between human and bovine serum albumins using flurbiprofen methyl ester as a probe. J. Phys. Chem. B 112, 2694 2699. (Pubitemid 351472979)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.9 , pp. 2694-2699
    • Vaya, I.1    Jimenez, M.C.2    Miranda, M.A.3
  • 5
    • 0030926943 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies on site-directed mutants of human serum albumin
    • DOI 10.1016/S0014-5793(97)00389-X, PII S001457939700389X
    • Helms, M. K., C. E. Peterson, N. V. Bhagvan D. M. Jameson (1997) Time-resolved fluorescence studies on site-directed mutants of human serum albumin. FEBS Lett. 408, 67 70. (Pubitemid 27216464)
    • (1997) FEBS Letters , vol.408 , Issue.1 , pp. 67-70
    • Helms, M.K.1    Petersen, C.E.2    Bhagavan, N.V.3    Jameson, D.M.4
  • 6
    • 34250840086 scopus 로고    scopus 로고
    • Relaxation dynamics of piroxicam structures within human serum albumin protein
    • DOI 10.1021/jm061421f
    • El.-Kernary, M., M. Gil A. Douhal (2007) Relaxation dynamics of piroxicam structures with human serum albumin protein. J. Med. Chem. 50, 2896 2902. (Pubitemid 46980860)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.12 , pp. 2896-2902
    • El-Kemary, M.1    Gil, M.2    Douhal, A.3
  • 7
    • 0021984733 scopus 로고
    • Relations between high affinity-binding sites of markers for binding regions of human serum albumin
    • Hansen, U. K. (1985) Relations between high affinity-binding sites of markers for binding regions of human serum albumin. Biochem. J. 225, 629 638.
    • (1985) Biochem. J. , vol.225 , pp. 629-638
    • Hansen, U.K.1
  • 8
    • 23844471367 scopus 로고    scopus 로고
    • Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine
    • DOI 10.1016/j.jphotobiol.2005.04.005, PII S1011134405001004
    • Hu, Y., Y. Liu, W. Jiang, R. Zhao S. Qu (2005) Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine. J. Photochem. Photobiol. B, Biol. 80, 235 242. (Pubitemid 41150653)
    • (2005) Journal of Photochemistry and Photobiology B: Biology , vol.80 , Issue.3 , pp. 235-242
    • Hu, Y.-J.1    Liu, Y.2    Jiang, W.3    Zhao, R.-M.4    Qu, S.-S.5
  • 10
    • 33646501452 scopus 로고    scopus 로고
    • Site-selective and dual mode recognition of serum albumin by a squarine dye
    • Jisha, V. S., K. T. Arun, M. Hariharan D. Ramaiah (2006) Site-selective and dual mode recognition of serum albumin by a squarine dye. J. Am. Chem. Soc. 128, 6024 6025.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6024-6025
    • Jisha, V.S.1    Arun, K.T.2    Hariharan, M.3    Ramaiah, D.4
  • 12
    • 20444395811 scopus 로고    scopus 로고
    • Photophysical properties of safranine and phenosafranine: A comparative study by laser flash photolysis and laser induced optoacoustic spectroscopy
    • Broglia, M. F., M. L. Gomez, S. G. Bertolotti, H. A. Montejano C. M. Previtalli (2005) Photophysical properties of safranine and phenosafranine: A comparative study by laser flash photolysis and laser induced optoacoustic spectroscopy. J. Photochem. Photobiol. A, Chem. 173, 115 120.
    • (2005) J. Photochem. Photobiol. A, Chem. , vol.173 , pp. 115-120
    • Broglia, M.F.1    Gomez, M.L.2    Bertolotti, S.G.3    Montejano, H.A.4    Previtalli, C.M.5
  • 13
    • 0030783486 scopus 로고    scopus 로고
    • Photoinduced energy and electron transfer between ketone triplets and organic dyes
    • Jockush, S., H. J. Timpe, W. Schnabel N. J. Turro (1997) Photoinduced energy and electron transfer between ketone triplets and organic dyes. J. Phys. Chem. A 101, 440 445. (Pubitemid 127591183)
    • (1997) Journal of Physical Chemistry A , vol.101 , Issue.4 , pp. 440-445
    • Jockusch, S.1    Timpe, H.-J.2    Schnabel, W.3    Turro, N.J.4
  • 14
    • 33748665023 scopus 로고    scopus 로고
    • Excited singlet state reaction of phenosafranine with electron donors: Role of the heavy-atom effect in triplet induction
    • Jayanthi, S. S. P. J. Ramamurthy (1998) Excited singlet state reaction of phenosafranine with electron donors: Role of the heavy-atom effect in triplet induction. Chem. Soc. Faraday Trans. 94, 1675 1679.
    • (1998) Chem. Soc. Faraday Trans. , vol.94 , pp. 1675-1679
    • Jayanthi, S.S.1    Ramamurthy, P.J.2
  • 15
    • 0001597509 scopus 로고
    • Photochemistry in polymers: Photoinduced electron transfer between phenosafranine and triethylamine in perfluorosulfonate membrane
    • Gopidas, K. R. P. V. Kamat (1990) Photochemistry in polymers: Photoinduced electron transfer between phenosafranine and triethylamine in perfluorosulfonate membrane. J. Phys. Chem. 94, 4723 4727.
    • (1990) J. Phys. Chem. , vol.94 , pp. 4723-4727
    • Gopidas, K.R.1    Kamat, P.V.2
  • 16
    • 49349105052 scopus 로고    scopus 로고
    • Binding interaction of cationic phenazinium dyes with calf thymus DNA: A comparative study
    • Sarkar, D., P. Das, S. Basak N. Chattopadhyay (2008) Binding interaction of cationic phenazinium dyes with calf thymus DNA: A comparative study. J. Phys. Chem. B 112, 9243 9249.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9243-9249
    • Sarkar, D.1    Das, P.2    Basak, S.3    Chattopadhyay, N.4
  • 17
    • 54849432774 scopus 로고    scopus 로고
    • Spectroscopic characterization of phenazinium dye aggregates in water and acetonitrile media: Effect of methyl substitution on the aggregation phenomenon
    • Sarkar, D., P. Das, A. Girigoswami N. Chattopadhyay (2008) Spectroscopic characterization of phenazinium dye aggregates in water and acetonitrile media: Effect of methyl substitution on the aggregation phenomenon. J. Phys. Chem. A 112, 9684 9691.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 9684-9691
    • Sarkar, D.1    Das, P.2    Girigoswami, A.3    Chattopadhyay, N.4
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248 254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 23844544802 scopus 로고    scopus 로고
    • Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine with serum albumins
    • DOI 10.1021/jp051367z
    • Mallick, A., B. Haldar N. Chattopadhyay (2005) Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H Indolo-[2,3-a] quinolizine with serum albumins. J. Phys. Chem. B 109, 14683 14690. (Pubitemid 41161744)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.30 , pp. 14683-14690
    • Mallick, A.1    Haldar, B.2    Chattopadhyay, N.3
  • 21
    • 17444407816 scopus 로고    scopus 로고
    • Photophysics in motionally constrained bioenvironment: Interaction of norharmane with bovine serum albumin
    • DOI 10.1562/2004-07-12-RA-230.1
    • Mallick, A. N. Chattopadhyay (2005) Photophysics in motionally constrained bioenvironment: Interaction of norharmane with bovine serum albumin. Photochem. Photobiol. 81, 419. (Pubitemid 40551520)
    • (2005) Photochemistry and Photobiology , vol.81 , Issue.2 , pp. 419-424
    • Mallick, A.1    Chattopadhyay, N.2
  • 22
    • 33947644936 scopus 로고    scopus 로고
    • Binding interaction of a biological photosensitizer with serum albumins: A biophysical study
    • DOI 10.1021/bm061084s
    • Chakrabarty, A., A. Mallick, B. Haldar, P. Das N. Chattopadhyay (2007) Binding interaction of a biological photosensitizer with serum albumins: A biophysical study. Biomacromolecules 8, 920 927. (Pubitemid 46488473)
    • (2007) Biomacromolecules , vol.8 , Issue.3 , pp. 920-927
    • Chakrabarty, A.1    Mallick, A.2    Haldar, B.3    Das, P.4    Chattopadhyay, N.5
  • 24
    • 33645929404 scopus 로고    scopus 로고
    • Solvatochromic effects on the fluorescence and triplet-triplet absorption of phenosafranine in protic and aprotic solvents
    • Broglia, M. F., S. G. Bertolotti, C. M. Previtalli H. A. Montejano (2006) Solvatochromic effects on the fluorescence and triplet-triplet absorption of phenosafranine in protic and aprotic solvents. J. Photochem. Photobiol. A, Chem. 180, 143 149.
    • (2006) J. Photochem. Photobiol. A, Chem. , vol.180 , pp. 143-149
    • Broglia, M.F.1    Bertolotti, S.G.2    Previtalli, C.M.3    Montejano, H.A.4
  • 25
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y. H., J. T. Yang H. M. Martinez (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120 4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 26
    • 35148890859 scopus 로고    scopus 로고
    • Photophysics of a cationic biological photosensitizer in anionic micellar environments: Combined effect of polarity and rigidity
    • DOI 10.1021/jp073984o
    • Das, P., A. Chakrabarty, A. Mallick N. Chattopadhyay (2007) Photophysics of a cationic biological photosensitizer in anionic micellar environments: Combined effect of polarity and rigidity. J. Phys. Chem. B 111, 11169. (Pubitemid 47548367)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.38 , pp. 11169-11176
    • Das, P.1    Chakrabarty, A.2    Mallick, A.3    Chattopadhyay, N.4
  • 27
    • 41849110995 scopus 로고    scopus 로고
    • Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: A spectroscopic study
    • DOI 10.1016/j.jphotobiol.2007.12.006, PII S101113440800002X
    • Balia Singh, R., S. Mohanta N. Guchhait (2008) Study of interaction of proton transfer probe 1-hydroxy-2-napthaldehyde with serum albumins: A spectroscopic study. J. Photochem. Photobiol. A, Chem. 91, 1 8. (Pubitemid 351494448)
    • (2008) Journal of Photochemistry and Photobiology B: Biology , vol.91 , Issue.1 , pp. 1-8
    • Balia Singh, R.1    Mahanta, S.2    Guchhait, N.3
  • 28
    • 0003141693 scopus 로고
    • Effect of cyclodextrin cavity size on twisted intramolecular charge transfer emission: Dimethylamino benzonitrile in β-cyclodextrin
    • Nag, A., R. Dutta, N. Chattopadhyay K. Bhattacharya (1989) Effect of cyclodextrin cavity size on twisted intramolecular charge transfer emission: Dimethylamino benzonitrile in β-cyclodextrin. Chem. Phys. Lett. 157, 83 86.
    • (1989) Chem. Phys. Lett. , vol.157 , pp. 83-86
    • Nag, A.1    Dutta, R.2    Chattopadhyay, N.3    Bhattacharya, K.4
  • 29
    • 65249136509 scopus 로고    scopus 로고
    • Interaction of bovine serum albumin with dipolar molecules: Fluorescence and molecular docking studies
    • Bhattacharya, B., S. Nakka, L. Guruprasad A. Samanta (2009) Interaction of bovine serum albumin with dipolar molecules: Fluorescence and molecular docking studies. J. Phys. Chem. B 113, 2143 2150.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2143-2150
    • Bhattacharya, B.1    Nakka, S.2    Guruprasad, L.3    Samanta, A.4
  • 30
    • 33746190548 scopus 로고
    • A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons
    • Benesi, M. L. J. H. Hildebrand (1949) A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. J. Am. Chem. Soc. 71, 2703 2707.
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 2703-2707
    • Benesi, M.L.1    Hildebrand, J.H.2
  • 32
    • 34547681744 scopus 로고    scopus 로고
    • Steady state fluorescence anisotropy to investigate flavonoids binding to proteins
    • Ingersoll, C. M. C. M. Strollo (2007) Steady state fluorescence anisotropy to investigate flavonoids binding to proteins. J. Chem. Educ. 84, 1313 1315.
    • (2007) J. Chem. Educ. , vol.84 , pp. 1313-1315
    • Ingersoll, C.M.1    Strollo, C.M.2
  • 33
    • 4143148584 scopus 로고    scopus 로고
    • Constrained photophysics of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine in micellar environments: A spectrofluorometric study
    • DOI 10.1016/j.jcis.2004.05.027, PII S0021979704004862
    • Mallick, A., B. Haldar, S. Maiti N. Chattopadhyay (2004) Constrained photophysics of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine in micellar environments: A spectrofluorometric study. J. Colloid Interface Sci. 278, 215 223. (Pubitemid 39094495)
    • (2004) Journal of Colloid and Interface Science , vol.278 , Issue.1 , pp. 215-223
    • Mallick, A.1    Haldar, B.2    Maiti, S.3    Chattopadhyay, N.4
  • 36
    • 34547394353 scopus 로고    scopus 로고
    • Effect of cyclodextrin nanocavity confinement on the photophysics of a β-carboline analogue: A spectroscopic study
    • DOI 10.1021/jp072142m
    • Das, P., A. Chakrabarty, B. Haldar, A. Mallick N. Chattopadhyay (2007) Effect of cyclodextrin nanocavity confinement on the photophysics of a β-carboline analogue: A spectroscopic study. J. Phys. Chem. B 111, 7401 7408. (Pubitemid 47160189)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.25 , pp. 7401-7408
    • Das, P.1    Chakrabarty, A.2    Haldar, B.3    Mallick, A.4    Chattopadhyay, N.5
  • 37
    • 5044238048 scopus 로고    scopus 로고
    • Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method
    • DOI 10.1021/bm049668m
    • Tian, J., J. Liu, W. He, Z. Hu, X. Yao X. Chen (2004) Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules 5, 1956 1961. (Pubitemid 39335237)
    • (2004) Biomacromolecules , vol.5 , Issue.5 , pp. 1956-1961
    • Tian, J.1    Liu, J.2    He, W.3    Hu, Z.4    Yao, X.5    Chen, X.6
  • 39
    • 34548850052 scopus 로고    scopus 로고
    • Steady state and time-resolved fluorescence investigation of the specific binding of two chlorin derivatives with human serum albumin
    • DOI 10.1021/jp072544u
    • Patel, S. A. Dutta (2007) Steady state and time-resolved fluorescence investigation of the specific binding of two chlorin derivatives with human serum albumin. J. Phys. Chem. B 111, 10557 10562. (Pubitemid 47441860)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.35 , pp. 10557-10562
    • Patel, S.1    Datta, A.2
  • 40
    • 0030780359 scopus 로고    scopus 로고
    • Rigidity of human α-fetoprotein tertiary structure is under ligand control
    • Uversky, V. N., N. V. Narizhneva, T. V. Ivanova A. Y. Tomashevski (1997) Rigidity of human α-fetoprotein tertiary structure is under ligand control. Biochemistry 36, 13638 13645.
    • (1997) Biochemistry , vol.36 , pp. 13638-13645
    • Uversky, V.N.1    Narizhneva, N.V.2    Ivanova, T.V.3    Tomashevski, A.Y.4
  • 41
    • 51849098535 scopus 로고    scopus 로고
    • Formation of a molten globule like state in bovine serum albumin at alkaline pH
    • Sen, P., B. Ahmad R. H. Khan (2008) Formation of a molten globule like state in bovine serum albumin at alkaline pH. Eur. Biophys. J. 37, 1303 1308.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 1303-1308
    • Sen, P.1    Ahmad, B.2    Khan, R.H.3
  • 42
    • 33646377871 scopus 로고    scopus 로고
    • Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: A novel approach directly assigning binding site
    • DOI 10.1021/bm050996b
    • Ahmad, B., S. Parveen R. H. Khan (2006) Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: A novel approach directly assigning binding site. Biomacromolecules 7, 1350 1356. (Pubitemid 43670828)
    • (2006) Biomacromolecules , vol.7 , Issue.4 , pp. 1350-1356
    • Ahmad, B.1    Parveen, S.2    Khan, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.