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Volumn 369, Issue 1-3, 2010, Pages 57-64

Fluorescence resonance energy transfer from serum albumins to 1-anthracene sulphonate entrapped in reverse micellar nanocavities

Author keywords

Circular dichroism; FRET; Protein folding; Quenching; Reverse micelles

Indexed keywords

ANTHRACENE; BINDING ENERGY; BODY FLUIDS; DYES; ENERGY TRANSFER; FLUORESCENCE; LAKES; MICELLES; PROBES; PROTEIN FOLDING; QUENCHING; RESONANCE; SODIUM;

EID: 77956878227     PISSN: 09277757     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2010.07.035     Document Type: Article
Times cited : (8)

References (56)
  • 1
    • 0005811494 scopus 로고    scopus 로고
    • Reverse micelles as a catalyst for the nucleophilic aromatic substitution between glutathione and 2, 4-dinitrochlorobenzene
    • Liou J.Y., Huang T.M., Chang G.G. Reverse micelles as a catalyst for the nucleophilic aromatic substitution between glutathione and 2, 4-dinitrochlorobenzene. J. Chem. Soc., Perkin Trans. 2 1999, 2171-2176.
    • (1999) J. Chem. Soc., Perkin Trans. 2 , pp. 2171-2176
    • Liou, J.Y.1    Huang, T.M.2    Chang, G.G.3
  • 2
    • 0032079936 scopus 로고    scopus 로고
    • A kinetic analysis of the endogenous lactate dehydrogenase activity of duck lens e{open}-crystallin in reverse micelles
    • Lee H.J., Chang G.G. A kinetic analysis of the endogenous lactate dehydrogenase activity of duck lens e{open}-crystallin in reverse micelles. J. Colloid Interface Sci. 1998, 201:26-33.
    • (1998) J. Colloid Interface Sci. , vol.201 , pp. 26-33
    • Lee, H.J.1    Chang, G.G.2
  • 3
    • 33748501255 scopus 로고    scopus 로고
    • Solvation dynamics of coumarin 480 in reverse micelles. Slow relaxation of water molecules
    • Sarkar N., Das K., Dutta A., Das S., Bhattacharya K. Solvation dynamics of coumarin 480 in reverse micelles. Slow relaxation of water molecules. J. Phys. Chem. 1996, 100:10523-10527.
    • (1996) J. Phys. Chem. , vol.100 , pp. 10523-10527
    • Sarkar, N.1    Das, K.2    Dutta, A.3    Das, S.4    Bhattacharya, K.5
  • 4
    • 0002293718 scopus 로고    scopus 로고
    • On the versatile surfactant Aerosol-OT (AOT): its physicochemical and surface chemical behaviours and uses
    • 62
    • Moulik S.P., Mukherjee K. On the versatile surfactant Aerosol-OT (AOT): its physicochemical and surface chemical behaviours and uses. Proc. Ind. Natl. Sci. Acad. 1996, A 62(3):215-222.
    • (1996) Proc. Ind. Natl. Sci. Acad. , Issue.3 A , pp. 215-222
    • Moulik, S.P.1    Mukherjee, K.2
  • 5
    • 0035807660 scopus 로고    scopus 로고
    • Photoinduced intermolecular electron transfer in micelles: dielectric and structural properties of micelle headgroup regions
    • A
    • Tavernier H.L., Laine F., Fayer M.D. Photoinduced intermolecular electron transfer in micelles: dielectric and structural properties of micelle headgroup regions. J. Phys. Chem. 2001, A 105:8944-8957.
    • (2001) J. Phys. Chem. , vol.105 , pp. 8944-8957
    • Tavernier, H.L.1    Laine, F.2    Fayer, M.D.3
  • 6
    • 0035137340 scopus 로고    scopus 로고
    • Origin of laurdan sensitivity to the vesicle-to-micelle transition of phospholipid-octylglucoside system: a time-resolved fluorescence study
    • Viard M., Gallay J., Vincent M., Paternostre M. Origin of laurdan sensitivity to the vesicle-to-micelle transition of phospholipid-octylglucoside system: a time-resolved fluorescence study. Biophys. J. 2001, 80:347-359.
    • (2001) Biophys. J. , vol.80 , pp. 347-359
    • Viard, M.1    Gallay, J.2    Vincent, M.3    Paternostre, M.4
  • 7
    • 0344862011 scopus 로고    scopus 로고
    • Solvation dynamics in DMPC vesicle in the presence of a protein
    • Dutta P., Sen S., Mukherjee S., Bhattacharyya K. Solvation dynamics in DMPC vesicle in the presence of a protein. Chem. Phys. Lett. 2003, 382:426-433.
    • (2003) Chem. Phys. Lett. , vol.382 , pp. 426-433
    • Dutta, P.1    Sen, S.2    Mukherjee, S.3    Bhattacharyya, K.4
  • 9
    • 44949250032 scopus 로고    scopus 로고
    • Recent developments in the application of nanoparticles prepared from w/o microemulsions in heterogeneous catalysis
    • Boutonnet M., Logdberg S., Svensson E.E. Recent developments in the application of nanoparticles prepared from w/o microemulsions in heterogeneous catalysis. Curr. Opin. Colloid Interface Sci. 2008, 13:270-286.
    • (2008) Curr. Opin. Colloid Interface Sci. , vol.13 , pp. 270-286
    • Boutonnet, M.1    Logdberg, S.2    Svensson, E.E.3
  • 10
    • 33644501147 scopus 로고    scopus 로고
    • The use of acridine orange base (AOB) as molecular probe to characterize nonaqueous AOT reverse micelles
    • Falcone R.D., Correa N.M., Biasutti M.A., Silber J.J. The use of acridine orange base (AOB) as molecular probe to characterize nonaqueous AOT reverse micelles. J. Colloid Interface Sci. 2006, 296:356-364.
    • (2006) J. Colloid Interface Sci. , vol.296 , pp. 356-364
    • Falcone, R.D.1    Correa, N.M.2    Biasutti, M.A.3    Silber, J.J.4
  • 11
    • 35948929053 scopus 로고    scopus 로고
    • Site-specific hydration status of an amphipathic peptide in AOT reverse micelles
    • Mukherjee S., Chowdhury P., DeGrado W.F., Gai F. Site-specific hydration status of an amphipathic peptide in AOT reverse micelles. Langmuir 2007, 23:11174-11179.
    • (2007) Langmuir , vol.23 , pp. 11174-11179
    • Mukherjee, S.1    Chowdhury, P.2    DeGrado, W.F.3    Gai, F.4
  • 12
    • 0030579816 scopus 로고    scopus 로고
    • The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-l-tryptophanamide
    • Davis D.M., McLoskey D., Birch D.J.S., Gellert P.R., Kittlety R.S., Swart R.M. The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-l-tryptophanamide. Biophys. Chem. 1996, 60:63-77.
    • (1996) Biophys. Chem. , vol.60 , pp. 63-77
    • Davis, D.M.1    McLoskey, D.2    Birch, D.J.S.3    Gellert, P.R.4    Kittlety, R.S.5    Swart, R.M.6
  • 13
    • 24344503784 scopus 로고    scopus 로고
    • Ultrafast dynamics in a nanocage of enzymes: solvation and fluorescence resonance energy transfer in reverse micelles
    • Majumder P., Sarkar R., Shaw A.K., Chakraborty A., Pal S.K. Ultrafast dynamics in a nanocage of enzymes: solvation and fluorescence resonance energy transfer in reverse micelles. J. Colloid Interface Sci. 2005, 290:462-474.
    • (2005) J. Colloid Interface Sci. , vol.290 , pp. 462-474
    • Majumder, P.1    Sarkar, R.2    Shaw, A.K.3    Chakraborty, A.4    Pal, S.K.5
  • 14
    • 0034309739 scopus 로고    scopus 로고
    • The location of tryptophan, N-acetyltryptophan and α-chymotrypsin in reverse micelles of AOT: a fluorescence study
    • Andrade S.M., Costa S.M.B. The location of tryptophan, N-acetyltryptophan and α-chymotrypsin in reverse micelles of AOT: a fluorescence study. Photochem. Photobiol. 2000, 72(4):444-450.
    • (2000) Photochem. Photobiol. , vol.72 , Issue.4 , pp. 444-450
    • Andrade, S.M.1    Costa, S.M.B.2
  • 15
    • 33747118682 scopus 로고    scopus 로고
    • Direct observation of protein folding in nanoenvironments using a molecular ruler
    • Sarkar R., Shaw A.K., Narayanan S.S., Dias F., Monk man A., Pal S.K. Direct observation of protein folding in nanoenvironments using a molecular ruler. Biophys. Chem. 2006, 123:40-48.
    • (2006) Biophys. Chem. , vol.123 , pp. 40-48
    • Sarkar, R.1    Shaw, A.K.2    Narayanan, S.S.3    Dias, F.4    Monk man, A.5    Pal, S.K.6
  • 16
    • 0346505325 scopus 로고    scopus 로고
    • Photodynamic effect of metallo 5-(4-carboxyphenyl)-10,15,20-tris (4-methylphenyl) porphyrins in biomimetic AOT reverse micelles containing urease
    • Scalise I., Durantini E.N. Photodynamic effect of metallo 5-(4-carboxyphenyl)-10,15,20-tris (4-methylphenyl) porphyrins in biomimetic AOT reverse micelles containing urease. J. Photochem. Photobiol. A: Chem. 2004, 162:105-113.
    • (2004) J. Photochem. Photobiol. A: Chem. , vol.162 , pp. 105-113
    • Scalise, I.1    Durantini, E.N.2
  • 18
    • 1242315445 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-a spectroscopic probe for organized surfactant media
    • De S., Girigoswami A. Fluorescence resonance energy transfer-a spectroscopic probe for organized surfactant media. J. Colloid Interface Sci. 2004, 271:485-495.
    • (2004) J. Colloid Interface Sci. , vol.271 , pp. 485-495
    • De, S.1    Girigoswami, A.2
  • 22
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin P.R. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 2000, 7:730-734.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 23
    • 4544237524 scopus 로고    scopus 로고
    • Visualization of molecular activities inside living cells with fluorescent labels
    • Bunt G., Wouters F.S. Visualization of molecular activities inside living cells with fluorescent labels. Int. Rev. Cytol. 2004, 237:205-277.
    • (2004) Int. Rev. Cytol. , vol.237 , pp. 205-277
    • Bunt, G.1    Wouters, F.S.2
  • 25
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • Min H.X., Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 1992, 358:209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • Min, H.X.1    Carter, D.C.2
  • 26
    • 0029924912 scopus 로고    scopus 로고
    • Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins
    • Moriyama Y., Ohta D., Hachiya K., Mitsui Y., Takeda K. Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins. J. Protein Chem. 1996, 15:265-272.
    • (1996) J. Protein Chem. , vol.15 , pp. 265-272
    • Moriyama, Y.1    Ohta, D.2    Hachiya, K.3    Mitsui, Y.4    Takeda, K.5
  • 27
    • 23844471367 scopus 로고    scopus 로고
    • Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine
    • Hu Y., Liu Y., Jiang W., Zhao R., Qu S. Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine. J. Photochem. Photobiol. B 2005, 80:235-242.
    • (2005) J. Photochem. Photobiol. B , vol.80 , pp. 235-242
    • Hu, Y.1    Liu, Y.2    Jiang, W.3    Zhao, R.4    Qu, S.5
  • 28
    • 33845904715 scopus 로고
    • Quenching of fluorescence of 2-anthracene sulphonate by cetylpyridinium chloride in micellar solutions of Tweens, Triton X-100, sodium dodecylsulphate (SDS) and cetyltrimethylammonium bromide (CTAB)
    • Bhattacharya S.C., Das H.T., Moulik S.P. Quenching of fluorescence of 2-anthracene sulphonate by cetylpyridinium chloride in micellar solutions of Tweens, Triton X-100, sodium dodecylsulphate (SDS) and cetyltrimethylammonium bromide (CTAB). J. Photochem. Photobiol. A: Chem. 1993, 71:257-262.
    • (1993) J. Photochem. Photobiol. A: Chem. , vol.71 , pp. 257-262
    • Bhattacharya, S.C.1    Das, H.T.2    Moulik, S.P.3
  • 29
    • 39149087662 scopus 로고    scopus 로고
    • Interaction of 1-anthracene sulphonate with cationic micelles of alkyl trimethyl ammonium bromides (CnTAB): a spectroscopic study
    • Sarkar A., Pramanik S., Banerjee P., Bhattacharya S.C. Interaction of 1-anthracene sulphonate with cationic micelles of alkyl trimethyl ammonium bromides (CnTAB): a spectroscopic study. Colloids Surf. A: Physicochem. Eng. Aspects 2008, 317:585-591.
    • (2008) Colloids Surf. A: Physicochem. Eng. Aspects , vol.317 , pp. 585-591
    • Sarkar, A.1    Pramanik, S.2    Banerjee, P.3    Bhattacharya, S.C.4
  • 30
    • 70349138804 scopus 로고    scopus 로고
    • Physicochemical characterization of reverse micelles of Triton X using 1-anthracene sulphonate as fluorescent probe: A spectroscopic study
    • Dhar S., Rana D.K., Sarkar A., Mandal T.K., Ghosh S., Bhattacharya S.C. Physicochemical characterization of reverse micelles of Triton X using 1-anthracene sulphonate as fluorescent probe: A spectroscopic study. Colloids Surf. A: Physicochem. Eng. Aspects 2009, 349:117-124.
    • (2009) Colloids Surf. A: Physicochem. Eng. Aspects , vol.349 , pp. 117-124
    • Dhar, S.1    Rana, D.K.2    Sarkar, A.3    Mandal, T.K.4    Ghosh, S.5    Bhattacharya, S.C.6
  • 31
    • 37849011178 scopus 로고    scopus 로고
    • Sulphonate derivatives of Naphtho[2,3-b]thiophen-4(9H)-one and 9(10H)-anthracenone as highly active antimicrotubule agents. synthesis antiproliferative activity, and inhibition of tubulin polymerization
    • Zuse A., Schmidt P., Baasner S., Böhm K.J., Müller K., Gerlach M., Günther E.G., Unger E., Prinz H. Sulphonate derivatives of Naphtho[2,3-b]thiophen-4(9H)-one and 9(10H)-anthracenone as highly active antimicrotubule agents. synthesis antiproliferative activity, and inhibition of tubulin polymerization. J. Med. Chem. 2007, 50:6059-6066.
    • (2007) J. Med. Chem. , vol.50 , pp. 6059-6066
    • Zuse, A.1    Schmidt, P.2    Baasner, S.3    Böhm, K.J.4    Müller, K.5    Gerlach, M.6    Günther, E.G.7    Unger, E.8    Prinz, H.9
  • 32
    • 49049109519 scopus 로고    scopus 로고
    • Electrogenerated chemiluminescence and its biorelated applications
    • Miao W Electrogenerated chemiluminescence and its biorelated applications. Chem. Rev. 2008, 108:2506-2553.
    • (2008) Chem. Rev. , vol.108 , pp. 2506-2553
    • Miao, W.1
  • 33
    • 5044239643 scopus 로고    scopus 로고
    • Molecular design, chemical synthesis, and biological evaluation of anthracene-carbohydrate hybrids as novel DNA photocleaving and photoselective cytotoxic agents
    • Toshima K., Hasegawa M., Shimizu J., Matsumura S. Molecular design, chemical synthesis, and biological evaluation of anthracene-carbohydrate hybrids as novel DNA photocleaving and photoselective cytotoxic agents. Arkivoc 2004, 13:28-35.
    • (2004) Arkivoc , vol.13 , pp. 28-35
    • Toshima, K.1    Hasegawa, M.2    Shimizu, J.3    Matsumura, S.4
  • 34
    • 58149105428 scopus 로고    scopus 로고
    • New development of reverse micelles and applications in protein separation and refolding
    • Yang L., Xiaoyan D., Yan S. New development of reverse micelles and applications in protein separation and refolding. Chin. J. Chem. Eng. 2008, 16(6):949-955.
    • (2008) Chin. J. Chem. Eng. , vol.16 , Issue.6 , pp. 949-955
    • Yang, L.1    Xiaoyan, D.2    Yan, S.3
  • 36
    • 0037118959 scopus 로고    scopus 로고
    • Light-harvesting supramolecular hydrogels assembled from short-legged cationic l-glutamate derivatives and anionic fluorophores
    • Nakashima T., Kimizuka N. Light-harvesting supramolecular hydrogels assembled from short-legged cationic l-glutamate derivatives and anionic fluorophores. Adv. Mater. 2002, 14:1113-1116.
    • (2002) Adv. Mater. , vol.14 , pp. 1113-1116
    • Nakashima, T.1    Kimizuka, N.2
  • 37
    • 33748323509 scopus 로고    scopus 로고
    • Anthracene-maleimide-based diels-alder " Click Chemistry" as a novel route to graft copolymers
    • Gacal B., Durmaz H., Tasdelen M.A., Hizal G., Tunca U., Yagci Y., Demirel A.L. Anthracene-maleimide-based diels-alder " Click Chemistry" as a novel route to graft copolymers. Macromolecules 2006, 39:5330-5336.
    • (2006) Macromolecules , vol.39 , pp. 5330-5336
    • Gacal, B.1    Durmaz, H.2    Tasdelen, M.A.3    Hizal, G.4    Tunca, U.5    Yagci, Y.6    Demirel, A.L.7
  • 38
    • 0011278157 scopus 로고
    • A Fourier transform infrared study of water-head group interactions in reversed micelles containing sodium bis (2-ethylhexyl) sulphosuccinate (AOT)
    • Christopher D.J., Yarwood J., Belton P.S., Hills B.P. A Fourier transform infrared study of water-head group interactions in reversed micelles containing sodium bis (2-ethylhexyl) sulphosuccinate (AOT). J. Colloid Interface Sci. 1992, 152:465-472.
    • (1992) J. Colloid Interface Sci. , vol.152 , pp. 465-472
    • Christopher, D.J.1    Yarwood, J.2    Belton, P.S.3    Hills, B.P.4
  • 40
    • 7044233615 scopus 로고    scopus 로고
    • Steady-state fluorescence and photophysical properties of a ketocyanine dye in binary surfactant and polymer-surfactant mixture
    • Shannigrahi M, Bagchi S. Steady-state fluorescence and photophysical properties of a ketocyanine dye in binary surfactant and polymer-surfactant mixture. J. Photochem. Photobiol. A: Chem. 2004, 168:133-141.
    • (2004) J. Photochem. Photobiol. A: Chem. , vol.168 , pp. 133-141
    • Shannigrahi, M.1    Bagchi, S.2
  • 41
    • 33845560552 scopus 로고
    • Dynamic and static aspects of solubilization of neutral arenes in ionic micellar solutions
    • Almgren M., Grieser F., Thomas J.K. Dynamic and static aspects of solubilization of neutral arenes in ionic micellar solutions. J. Am. Chem. Soc. 1979, 101:279-291.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 279-291
    • Almgren, M.1    Grieser, F.2    Thomas, J.K.3
  • 42
    • 70349237017 scopus 로고    scopus 로고
    • Deciphering the fluorescence resonance energy transfer signature of 3-pyrazolyl 2-pyrazoline in transport proteinous environment
    • Banerjee P., Pramanik S., Sarkar A., Bhattacharya S.C. Deciphering the fluorescence resonance energy transfer signature of 3-pyrazolyl 2-pyrazoline in transport proteinous environment. J. Phys. Chem. B 2009, 113:11429-11436.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11429-11436
    • Banerjee, P.1    Pramanik, S.2    Sarkar, A.3    Bhattacharya, S.C.4
  • 43
    • 47749100432 scopus 로고    scopus 로고
    • PEGylation of human serum albumin: reaction of PEG-phenyl-isothiocyanate with protein
    • Meng F., Manjula B.N., Smith P.K., Acharya S.A. PEGylation of human serum albumin: reaction of PEG-phenyl-isothiocyanate with protein. Bioconjug. Chem. 2008, 19(7):1352-1360.
    • (2008) Bioconjug. Chem. , vol.19 , Issue.7 , pp. 1352-1360
    • Meng, F.1    Manjula, B.N.2    Smith, P.K.3    Acharya, S.A.4
  • 44
    • 0000439983 scopus 로고
    • Size and mobility of sodium dodecyl sulphate-bovine serum albumin complex as studied by dynamic light scattering and electrophoretic light scattering
    • Takeda K., Sasaoka H., Sasa K., Hirai H., Hachiya K., Moriyama Y. Size and mobility of sodium dodecyl sulphate-bovine serum albumin complex as studied by dynamic light scattering and electrophoretic light scattering. J. Colloid Interface Science 1992, 154:385-392.
    • (1992) J. Colloid Interface Science , vol.154 , pp. 385-392
    • Takeda, K.1    Sasaoka, H.2    Sasa, K.3    Hirai, H.4    Hachiya, K.5    Moriyama, Y.6
  • 45
    • 0017661379 scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin
    • Sklar L.A., Hudson B.S., Simoni R.D. Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochemistry 1977, 16:5100-5108.
    • (1977) Biochemistry , vol.16 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 46
    • 0036434544 scopus 로고    scopus 로고
    • The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study
    • Sengupta B., Sengupta P.K. The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study. Biochem. Biophys. Res. Commun. 2002, 299:400-403.
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 400-403
    • Sengupta, B.1    Sengupta, P.K.2
  • 47
    • 45949100016 scopus 로고    scopus 로고
    • Energy transfer photophysics from serum albumins to sequestered 3-hydroxy-2-naphthoic acid, an excited state intramolecular proton-transfer probe
    • Saha Sardar P., Samanta S., Maity S.S., Dasgupta S., Ghosh S. Energy transfer photophysics from serum albumins to sequestered 3-hydroxy-2-naphthoic acid, an excited state intramolecular proton-transfer probe. J. Phys. Chem. B 2008, 112:3451-3461.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3451-3461
    • Saha Sardar, P.1    Samanta, S.2    Maity, S.S.3    Dasgupta, S.4    Ghosh, S.5
  • 48
    • 0042764667 scopus 로고    scopus 로고
    • Competition between energy transfer and deactivation during quenching of tryptophan fluorescence of albumin by dye molecules
    • Vekshin N.L., Sukharev V.I., van Hoek A., Visser A.J.W.G. Competition between energy transfer and deactivation during quenching of tryptophan fluorescence of albumin by dye molecules. J. Fluoresc. 1999, 9:99-101.
    • (1999) J. Fluoresc. , vol.9 , pp. 99-101
    • Vekshin, N.L.1    Sukharev, V.I.2    van Hoek, A.3    Visser, A.J.W.G.4
  • 49
    • 0032495131 scopus 로고    scopus 로고
    • Investigation of the interaction between acridine orange and bovine serum albumin
    • Feng X.Z., Lin Z., Yang L.J., Wang C., Bai C.L. Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 1998, 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
  • 50
    • 0001363954 scopus 로고
    • Time-resolved fluorescence techniques: methods and applications in biology
    • Prendergast F.G. Time-resolved fluorescence techniques: methods and applications in biology. Curr. Opin. Struct. Biol. 1991, 1:1054-1059.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 1054-1059
    • Prendergast, F.G.1
  • 52
    • 23844444530 scopus 로고    scopus 로고
    • Photophysical study of 3-Acetyl-4-oxo-6, 7-dihydro-12H-indolo[2,3-a]quinolizine in biomimetic reverse micellar nanocavities: A spectroscopic approach
    • Mallick A., Haldar B., Maiti S., Bera S.C., Chattopadhyay N. Photophysical study of 3-Acetyl-4-oxo-6, 7-dihydro-12H-indolo[2,3-a]quinolizine in biomimetic reverse micellar nanocavities: A spectroscopic approach. J. Phys. Chem. B 2005, 109:14675-14682.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 14675-14682
    • Mallick, A.1    Haldar, B.2    Maiti, S.3    Bera, S.C.4    Chattopadhyay, N.5
  • 53
    • 66349101345 scopus 로고    scopus 로고
    • Spectroscopic investigations of the binding interaction of a new indanedione derivative with human and bovine serum albumins
    • Stan D., Matei I., Mihailescu C., Savin M., Matache M., Hillebrand M., Baciu I. Spectroscopic investigations of the binding interaction of a new indanedione derivative with human and bovine serum albumins. Molecules 2009, 14:1614-1626.
    • (2009) Molecules , vol.14 , pp. 1614-1626
    • Stan, D.1    Matei, I.2    Mihailescu, C.3    Savin, M.4    Matache, M.5    Hillebrand, M.6    Baciu, I.7
  • 54
    • 4444325241 scopus 로고    scopus 로고
    • The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods
    • Gao H., Lei L.D., Liu J.Q., Kong Q., Chen X.G., Hu Z.D. The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods. J. Photochem. Photobiol. A: Chem. 2004, 167:213-221.
    • (2004) J. Photochem. Photobiol. A: Chem. , vol.167 , pp. 213-221
    • Gao, H.1    Lei, L.D.2    Liu, J.Q.3    Kong, Q.4    Chen, X.G.5    Hu, Z.D.6
  • 56
    • 48349123224 scopus 로고    scopus 로고
    • Structural effects of nogalamycin, an antibiotic antitumour agent, on DNA
    • Banerjee T., Mukhopadhyay R. Structural effects of nogalamycin, an antibiotic antitumour agent, on DNA. Biochem. Biophys. Res. Commun. 2008, 374:264-268.
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 264-268
    • Banerjee, T.1    Mukhopadhyay, R.2


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