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Volumn 102, Issue 1, 2011, Pages 11-19

Investigations on the interactions of aurintricarboxylic acid with bovine serum albumin: Steady state/time resolved spectroscopic and docking studies

Author keywords

Bovine serum albumin; Circular dichroism; Hydrophobic interaction; Molecular docking; Static mode; Time resolved spectroscopy

Indexed keywords

AURINTRICARBOXYLIC ACID; BOVINE SERUM ALBUMIN;

EID: 78650861803     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2010.08.011     Document Type: Article
Times cited : (52)

References (54)
  • 1
    • 0027260453 scopus 로고
    • Internucleosomal DNA cleavage and neuronal cell survival/death
    • A. Batistatou, and L.A. Greene Internucleosomal DNA cleavage and neuronal cell survival/death J. Cell Biol. 122 1993 523 532
    • (1993) J. Cell Biol. , vol.122 , pp. 523-532
    • Batistatou, A.1    Greene, L.A.2
  • 2
    • 0027071804 scopus 로고
    • Nerve growth factor withdrawal-induced cell death in neuronal PC12 cells resembles that in sympathetic neurons
    • P.W. Mesner, T.R. Winters, and S.H. Green Nerve growth factor withdrawal-induced cell death in neuronal PC12 cells resembles that in sympathetic neurons J. Cell Biol. 119 1992 1669 1680
    • (1992) J. Cell Biol. , vol.119 , pp. 1669-1680
    • Mesner, P.W.1    Winters, T.R.2    Green, S.H.3
  • 3
    • 0036085386 scopus 로고    scopus 로고
    • Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition
    • C.J. Tsi, Y. Chao, C.W. Chen, and W.W. Lin Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition Mol. Pharmacol. 62 2002 90 101
    • (2002) Mol. Pharmacol. , vol.62 , pp. 90-101
    • Tsi, C.J.1    Chao, Y.2    Chen, C.W.3    Lin, W.W.4
  • 4
    • 0036171227 scopus 로고    scopus 로고
    • Aurintricarboxylic acid induces a distinct activation of the IGF-I receptor signaling within MDA-231 Cells
    • M. Haimsohn, R. Beery, A. Karasik, H. Kanety, and A. Geiger Aurintricarboxylic acid induces a distinct activation of the IGF-I receptor signaling within MDA-231 Cells Endocrinology 143 2002 837 845
    • (2002) Endocrinology , vol.143 , pp. 837-845
    • Haimsohn, M.1    Beery, R.2    Karasik, A.3    Kanety, H.4    Geiger, A.5
  • 5
    • 0025223232 scopus 로고
    • Aurintricarboxylic acid, the anti-aids compound, prevents the binding of interferon α-to its receptor
    • Y.X. Gan, J.L. Weaver, P.S. Pine, K.C. Zoon, and A. Aszalos Aurintricarboxylic acid, the anti-aids compound, prevents the binding of interferon α-to its receptor Biochem. Biophys. Res. Commun. 172 1990 1298 1303
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 1298-1303
    • Gan, Y.X.1    Weaver, J.L.2    Pine, P.S.3    Zoon, K.C.4    Aszalos, A.5
  • 6
    • 0017760663 scopus 로고
    • Effect of aurintricarboxylic acid on in vitro DNA synthetic activity of mouse sarcoma cells
    • S. Seki, K. Tsutsui, and T. Oda Effect of aurintricarboxylic acid on in vitro DNA synthetic activity of mouse sarcoma cells Biochem. Biophys. Res. Commun. 79 1977 179 184
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 179-184
    • Seki, S.1    Tsutsui, K.2    Oda, T.3
  • 7
    • 0023757086 scopus 로고
    • Differential inhibition of various deoxyribonucleic acid polymerases by Evans blue and aurintricalboxylic acid
    • H. Nakane, J. Balzarini, E. De Clercq, and K. Ono Differential inhibition of various deoxyribonucleic acid polymerases by Evans blue and aurintricalboxylic acid Eur. J. Biochem. 177 1988 91 96
    • (1988) Eur. J. Biochem. , vol.177 , pp. 91-96
    • Nakane, H.1    Balzarini, J.2    De Clercq, E.3    Ono, K.4
  • 8
  • 9
    • 0026046948 scopus 로고
    • Aurintricarboxylic acid rescues PC12 cells and sympathetic neurons from cell death caused by nerve growth factor deprivation: Correlation with suppression of endonuclease activity
    • A. Batistatou, and L.A. Greene Aurintricarboxylic acid rescues PC12 cells and sympathetic neurons from cell death caused by nerve growth factor deprivation: correlation with suppression of endonuclease activity J. Cell Biol. 115 1991 461 471
    • (1991) J. Cell Biol. , vol.115 , pp. 461-471
    • Batistatou, A.1    Greene, L.A.2
  • 10
    • 0017669601 scopus 로고
    • Use of aurintricarboxylic acid as an inhibitor of nucleases during nucleic acid isolation
    • R.B. Hallick, B.K. Chelm, P.W. Gray, and E.M. Orozco Use of aurintricarboxylic acid as an inhibitor of nucleases during nucleic acid isolation Nucleic Acids Res. 4 1977 3055 3064
    • (1977) Nucleic Acids Res. , vol.4 , pp. 3055-3064
    • Hallick, R.B.1    Chelm, B.K.2    Gray, P.W.3    Orozco, E.M.4
  • 11
    • 0028070221 scopus 로고
    • Inhibition of topoisomerase II by aurintricarboxylic acid: Implication for mechanism of apoptosis
    • D.R. Catchpoole, and B.W. Stewart Inhibition of topoisomerase II by aurintricarboxylic acid: implication for mechanism of apoptosis Anticancer Res. 14 1994 853 856
    • (1994) Anticancer Res. , vol.14 , pp. 853-856
    • Catchpoole, D.R.1    Stewart, B.W.2
  • 12
    • 0017226202 scopus 로고
    • Aurintricarboxylic acid is a nonspecific enzyme inhibitor
    • M. Bina-Stein, and T.R. Tritton Aurintricarboxylic acid is a nonspecific enzyme inhibitor Mol. Pharmacol. 12 1976 191 193
    • (1976) Mol. Pharmacol. , vol.12 , pp. 191-193
    • Bina-Stein, M.1    Tritton, T.R.2
  • 13
    • 0028896030 scopus 로고
    • Aurintricarboxilic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells
    • Y. Benchokroun, J. Couprie, and A.K. Larsen Aurintricarboxilic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells Biochem. Pharmacol. 49 1995 305 313
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 305-313
    • Benchokroun, Y.1    Couprie, J.2    Larsen, A.K.3
  • 14
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X. M He, and D.C. Carter Atomic structure and chemistry of human serum albumin Nature 358 1992 209 215
    • (1992) Nature , vol.358 , pp. 209-215
    • He X, M.1    Carter, D.C.2
  • 16
  • 17
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • C. Dufour, and O. Dangles Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy Biochim. Biophys. Acta 1721 2005 164 173
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 18
    • 67650485776 scopus 로고    scopus 로고
    • Interaction of the docetaxel with human serum albumin using optical spectroscopy methods
    • H. Cheng, H. Liu, Y. Zhang, and G. Zou Interaction of the docetaxel with human serum albumin using optical spectroscopy methods J. Lumin. 129 2009 1196 1203
    • (2009) J. Lumin. , vol.129 , pp. 1196-1203
    • Cheng, H.1    Liu, H.2    Zhang, Y.3    Zou, G.4
  • 19
    • 71549137169 scopus 로고    scopus 로고
    • Study of the interaction between fluoxetine hydrochloride and bovine serum albumin in the imitated physiological conditions by multi-spectroscopic methods
    • U. Katrahalli, U.S. Jaldappagari, and S.S. Kalanur Study of the interaction between fluoxetine hydrochloride and bovine serum albumin in the imitated physiological conditions by multi-spectroscopic methods J. Lumin. 130 2010 211 216
    • (2010) J. Lumin. , vol.130 , pp. 211-216
    • Katrahalli, U.1    Jaldappagari, U.S.2    Kalanur, S.S.3
  • 20
    • 41949108321 scopus 로고    scopus 로고
    • Molecular interactions between Wells-Dawson type polyoxometalates and human serum albumin
    • DOI 10.1021/bm701120j
    • G. Zhang, B. Keita, C.T. Craescu, S. Miron, P. Oliveira, and L. Nadjo Molecular interactions between Wells-Dawson type polyoxometalates and human serum albumin Biomacromolecules 9 2008 812 817 (Pubitemid 351560470)
    • (2008) Biomacromolecules , vol.9 , Issue.3 , pp. 812-817
    • Zhang, G.1    Keita, B.2    Craescu, C.T.3    Miron, S.4    De Oliveira, P.5    Nadjo, L.6
  • 21
    • 41849121510 scopus 로고    scopus 로고
    • New approach to measure protein binding based on a parallel artificial membrane assay and human serum albumin
    • E. Lázaro, P.J. Lowe, X. Briand, and B. Faller New approach to measure protein binding based on a parallel artificial membrane assay and human serum albumin J. Med. Chem. 51 2008 2009 2017
    • (2008) J. Med. Chem. , vol.51 , pp. 2009-2017
    • Lázaro, E.1    Lowe, P.J.2    Briand, X.3    Faller, B.4
  • 22
  • 23
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • U. Kragh-Hansen Molecular aspects of ligand binding to serum albumin Pharmacol. Rev. 33 1981 17 53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 24
    • 14744268162 scopus 로고    scopus 로고
    • Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin
    • DOI 10.1016/j.molstruc.2004.11.062, PII S0022286004009627
    • Y.J. Hu, Y. Liu, X.S. Shen, X.Y. Fang, and S.S. Qu Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin J. Mol. Struct. 738 2005 143 147 (Pubitemid 40326171)
    • (2005) Journal of Molecular Structure , vol.738 , Issue.1-3 , pp. 143-147
    • Hu, Y.-J.1    Liu, Y.2    Shen, X.-S.3    Fang, X.-Y.4    Qu, S.-S.5
  • 25
    • 0642316329 scopus 로고    scopus 로고
    • Interaction of magnolol with bovine serum albumin: A fluorescence- quenching study
    • DOI 10.1007/s00216-003-2017-8
    • L. Jiaquin, T. Jianniao, J. Zhang, Z. Hu, and C. Xingguo Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study Anal. Bioanal. Chem. 376 2003 864 867 (Pubitemid 40877950)
    • (2003) Analytical and Bioanalytical Chemistry , vol.376 , Issue.6 , pp. 864-867
    • Liu, J.1    Tian, J.-N.2    Zhang, J.3    Hu, Z.4    Chen, X.5
  • 28
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • M.B. Rarey, B. Kramer, T. Lengauer, and G. Klebe A fast flexible docking method using an incremental construction algorithm J. Mol. Biol. 261 1996 470 489
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.B.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 30
    • 0032518052 scopus 로고    scopus 로고
    • Investigations of excited state quenching reactions between p-toluidine, its N,N-dimethyl derivative and the acceptor dimethylterapthalate at different temperatures
    • S. Sinha, R. De, and T. Ganguly Investigations of excited state quenching reactions between p-toluidine, its N,N-dimethyl derivative and the acceptor dimethylterapthalate at different temperatures J. Photochem. Photobiol. A: Chem. 112 1998 13 20
    • (1998) J. Photochem. Photobiol. A: Chem. , vol.112 , pp. 13-20
    • Sinha, S.1    De, R.2    Ganguly, T.3
  • 31
    • 0002388667 scopus 로고
    • On the quenching-time of fluorescence
    • O. Stern, and M. Volmer On the quenching-time of fluorescence Phys. Z 20 1919 183 188
    • (1919) Phys. Z , vol.20 , pp. 183-188
    • Stern, O.1    Volmer, M.2
  • 34
    • 0037436982 scopus 로고    scopus 로고
    • Photophysics of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine: Emission from two states
    • A. Mallick, S. Maiti, B. Haldar, P. Purkayastha, and N. Chattopadhyay Photophysics of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine: emission from two states Chem. Phys. Lett. 371 2003 688 693
    • (2003) Chem. Phys. Lett. , vol.371 , pp. 688-693
    • Mallick, A.1    Maiti, S.2    Haldar, B.3    Purkayastha, P.4    Chattopadhyay, N.5
  • 37
    • 52649126204 scopus 로고    scopus 로고
    • Urea-induced denaturation of human serum albumin labeled with acrylodan
    • J. Gonzalez-Jimenez, and M. Cortijo Urea-induced denaturation of human serum albumin labeled with acrylodan J. Protein Chem. 21 2002 75 79
    • (2002) J. Protein Chem. , vol.21 , pp. 75-79
    • Gonzalez-Jimenez, J.1    Cortijo, M.2
  • 38
    • 0038408836 scopus 로고    scopus 로고
    • Effect of urea on serum albumin complex with antithyroid drugs: Fluorescence study
    • A. Sulkowska, B. Bojko, J. Rownicka, D. Pentak, and W. Sulkowski Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study J. Mol. Struct. 651-653 2003 237 243
    • (2003) J. Mol. Struct. , vol.651-653 , pp. 237-243
    • Sulkowska, A.1    Bojko, B.2    Rownicka, J.3    Pentak, D.4    Sulkowski, W.5
  • 39
    • 0023388641 scopus 로고
    • Urea-induced structural transformations in bovine serum albumin
    • M.Y. Khan, S.K. Agarwal, and S.J. Hangloo Urea-induced structural transformations in bovine serum albumin Biochemistry 102 1987 313 317
    • (1987) Biochemistry , vol.102 , pp. 313-317
    • Khan, M.Y.1    Agarwal, S.K.2    Hangloo, S.J.3
  • 40
    • 0346095165 scopus 로고    scopus 로고
    • Intermediate formation at lower urea concentration in "b" isomer of human serum albumin: A case study using domain specific ligands
    • B. Ahmad, M.K.A. Khan, S.K. Haq, and R.H. Khan Intermediate formation at lower urea concentration in "B" isomer of human serum albumin: a case study using domain specific ligands Biochem. Biophys. Res. Commun. 314 2004 166 173
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 166-173
    • Ahmad, B.1    Khan, M.K.A.2    Haq, S.K.3    Khan, R.H.4
  • 41
    • 77649244339 scopus 로고    scopus 로고
    • Fluorescent probing of urea-induced chemical unfolding of bovine serum albumin by intramolecular charge transfer fluorescence probe E-3-(4-dimethylamino-naphthalen-1-yl)-acrylic acid
    • S. Ghosh, and N. Guchhait Fluorescent probing of urea-induced chemical unfolding of bovine serum albumin by intramolecular charge transfer fluorescence probe E-3-(4-dimethylamino-naphthalen-1-yl)-acrylic acid Photochem. Photobiol. 86 2010 290 296
    • (2010) Photochem. Photobiol. , vol.86 , pp. 290-296
    • Ghosh, S.1    Guchhait, N.2
  • 42
    • 0006865931 scopus 로고    scopus 로고
    • Action of urea on the microheterogeneous environments. A model for expulsion of the probe from its preferred site
    • N. Chattopadhya Action of urea on the microheterogeneous environments. A model for expulsion of the probe from its preferred site ACH Models Chem. 134 1997 129 140
    • (1997) ACH Models Chem. , vol.134 , pp. 129-140
    • Chattopadhya, N.1
  • 43
    • 72449130909 scopus 로고    scopus 로고
    • Fluorescence spectroscopic characterization of the interaction of human adult hemoglobin and two isatins, 1-methylisatin and 1 phenylisatin: A comparative study
    • P. Mandal, and T. Ganguly Fluorescence spectroscopic characterization of the interaction of human adult hemoglobin and two isatins, 1-methylisatin and 1 phenylisatin: a comparative study J. Phys. Chem. B 113 2009 14904 14913
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14904-14913
    • Mandal, P.1    Ganguly, T.2
  • 44
    • 0345328130 scopus 로고    scopus 로고
    • Photophysical studies on binding of curcumin to bovin serum albumin
    • A. Barik, K.I. Priyadarsini, and H. Mohal Photophysical studies on binding of curcumin to bovin serum albumin Photochem. Photobiol. 77 2003 597 603
    • (2003) Photochem. Photobiol. , vol.77 , pp. 597-603
    • Barik, A.1    Priyadarsini, K.I.2    Mohal, H.3
  • 46
    • 0036179299 scopus 로고    scopus 로고
    • Toward reagent free clinical analysis: Quantitation of urine urea, creatinine, and total protein from the mid-infrared spectra of dried urine films
    • K. Liu, R. A Shaw, A. Man, T.C. Demibinski, and H.H. Mantsch Toward reagent free clinical analysis: quantitation of urine urea, creatinine, and total protein from the mid-infrared spectra of dried urine films Clin. Chem. 48 2002 499 506
    • (2002) Clin. Chem. , vol.48 , pp. 499-506
    • Liu, K.1    Shaw R, A.2    Man, A.3    Demibinski, T.C.4    Mantsch, H.H.5
  • 47
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 486
    • (1986) Biopolymers , vol.25 , pp. 469-486
    • Byler, D.M.1    Susi, H.2
  • 48
    • 33947688790 scopus 로고    scopus 로고
    • 4 based nanocomposite featuring direct electron transfer and peroxidase activity
    • 4 based nanocomposite featuring direct electron transfer and peroxidase activity J. Mater. Chem. 17 2007 1427 1432
    • (2007) J. Mater. Chem. , vol.17 , pp. 1427-1432
    • Lu, X.1    Zoua, G.2    Li, J.3
  • 49
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subhramanian Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 1981 096 3102
    • (1981) Biochemistry , vol.20 , pp. 096-3102
    • Ross, P.D.1    Subhramanian, S.2
  • 50
    • 7044231247 scopus 로고    scopus 로고
    • Interactions of human serum albumin with chlorogenic acid and ferulic acid
    • J. Kang, Y. Liu, M.X. Xie, S. Li, M. Jiang, and Y.D. Wang Interactions of human serum albumin with chlorogenic acid and ferulic acid Biochim. Biophys. Acta 1674 2004 205 214
    • (2004) Biochim. Biophys. Acta , vol.1674 , pp. 205-214
    • Kang, J.1    Liu, Y.2    Xie, M.X.3    Li, S.4    Jiang, M.5    Wang, Y.D.6
  • 51
    • 0346058044 scopus 로고    scopus 로고
    • Interaction of isofraxidin with human serum albumin
    • J.Q. Liu, J.N. Tian, and X. Tian Interaction of isofraxidin with human serum albumin Bioorg. Med. Chem. 12 2004 469 474
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 469-474
    • Liu, J.Q.1    Tian, J.N.2    Tian, X.3
  • 53
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • N. Brandes, P.B. Welzel, C. Werner, and L.W. Kroh Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis J. Colloid Interface Sci. 299 2006 56 69
    • (2006) J. Colloid Interface Sci. , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 54
    • 0018903487 scopus 로고
    • Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinimide fluorescence quenching
    • B.F. Peterman, and K.J. Laidler Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinimide fluorescence quenching Arch. Biochem. Biophys. 199 1980 158 164
    • (1980) Arch. Biochem. Biophys. , vol.199 , pp. 158-164
    • Peterman, B.F.1    Laidler, K.J.2


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