메뉴 건너뛰기




Volumn 38, Issue 2, 2014, Pages 595-606

Exploring the interactions of decabrominateddiphenyl ether and tetrabromobisphenol A with human serum albumin

Author keywords

Binding interaction; Brominated flame retardants; Decabrominateddiphenyl ether; Human serum albumin; Tetrabromobisphenol A

Indexed keywords

DECABROMINATEDDIPHENYL ETHER; DIPHENYL ETHER; FLAME RETARDANT; HUMAN SERUM ALBUMIN; TETRABROMOBISPHENOL A; UNCLASSIFIED DRUG; DECABROMOBIPHENYL ETHER; DIPHENYL ETHER DERIVATIVE; POLYBROMINATED BIPHENYL; PROTEIN BINDING; SERUM ALBUMIN;

EID: 84908461225     PISSN: 13826689     EISSN: 18727077     Source Type: Journal    
DOI: 10.1016/j.etap.2014.08.009     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 84880470765 scopus 로고    scopus 로고
    • Spectroscopy of hydroxyphenyl benzazoles in solution and human serum albumin: detecting flexibility, specificity and high affinity of the warfarin drug binding site
    • Abou-Zied O.K. Spectroscopy of hydroxyphenyl benzazoles in solution and human serum albumin: detecting flexibility, specificity and high affinity of the warfarin drug binding site. RCS Adv. 2013, 3:8747-8755.
    • (2013) RCS Adv. , vol.3 , pp. 8747-8755
    • Abou-Zied, O.K.1
  • 2
    • 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
    • Ahmad B., Khan M.K., Haq S.K., Khan R.H. Intermediate formation at lower urea concentration in 'B' isomer of human serum albumin: a case study using domain specific ligands. Biochem. Biophys. Res. Commun. 2004, 314:166-173.
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 166-173
    • Ahmad, B.1    Khan, M.K.2    Haq, S.K.3    Khan, R.H.4
  • 3
    • 30344452284 scopus 로고    scopus 로고
    • Photodegradation of decabromoiphenyl ether adsorbed onto clay minerals, metal oxides, and sediment
    • Ahn M.Y., Filley T.R., Jafvert C.T., Nies L., Hua I., Bezares-Cruz J. Photodegradation of decabromoiphenyl ether adsorbed onto clay minerals, metal oxides, and sediment. Environ. Sci. Technol. 2006, 40:215-220.
    • (2006) Environ. Sci. Technol. , vol.40 , pp. 215-220
    • Ahn, M.Y.1    Filley, T.R.2    Jafvert, C.T.3    Nies, L.4    Hua, I.5    Bezares-Cruz, J.6
  • 4
    • 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 X., Zhang H.Q. Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochim. Acta A 2005, 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, X.5    Zhang, H.Q.6
  • 6
    • 0017294689 scopus 로고
    • Binding of digitoxin to human serum albumin: influence of free fatty acids, bile acids, and protein unfolding on the digitoxin-albumin interaction
    • Brock A. Binding of digitoxin to human serum albumin: influence of free fatty acids, bile acids, and protein unfolding on the digitoxin-albumin interaction. Acta Pharmacol. Toxicol. 1976, 38:497-507.
    • (1976) Acta Pharmacol. Toxicol. , vol.38 , pp. 497-507
    • Brock, A.1
  • 8
    • 0030749791 scopus 로고    scopus 로고
    • Identification of subdomain IB in human serum albumin as a major binding site for polycyclic aromatic hydrocarbon epoxides
    • Brunmark P., Harriman S., Skipper P.L., Wishnok J.S., Amin S., Tannenbaum S.R. Identification of subdomain IB in human serum albumin as a major binding site for polycyclic aromatic hydrocarbon epoxides. Chem. Res. Toxicol. 1997, 10:880-886.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 880-886
    • Brunmark, P.1    Harriman, S.2    Skipper, P.L.3    Wishnok, J.S.4    Amin, S.5    Tannenbaum, S.R.6
  • 9
    • 84888033883 scopus 로고    scopus 로고
    • Inhibition of thyroid hormone sulfotransferase activity by brominated flame retardants and halogenated phenolics
    • Butt C.M., Stapleton H.M. Inhibition of thyroid hormone sulfotransferase activity by brominated flame retardants and halogenated phenolics. Chem. Res. Toxicol. 2013, 26:1692-1702.
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 1692-1702
    • Butt, C.M.1    Stapleton, H.M.2
  • 10
    • 26844560729 scopus 로고    scopus 로고
    • Effects of the brominated flame retardant tetrabromobisphenol-A (TBBPA) on cell signaling and function of Mytilus hemocytes: involvement of MAP kinases and protein kinase C
    • Canesi L., Lorusso L.C., Ciacci C., Betti M., Gallo G. Effects of the brominated flame retardant tetrabromobisphenol-A (TBBPA) on cell signaling and function of Mytilus hemocytes: involvement of MAP kinases and protein kinase C. Aquat. Toxicol. 2005, 75:277-287.
    • (2005) Aquat. Toxicol. , vol.75 , pp. 277-287
    • Canesi, L.1    Lorusso, L.C.2    Ciacci, C.3    Betti, M.4    Gallo, G.5
  • 11
    • 84908419917 scopus 로고    scopus 로고
    • Molegro Molecular Viewer 2012 2.5.0.
    • CLC Drug Discovery Workbench. Molegro Molecular Viewer 2012 2.5.0. http://www.clcbio.com/products/molegro.
  • 12
    • 0345179962 scopus 로고    scopus 로고
    • The stability of cyclodextrin complexes in solution
    • Connors K.A. The stability of cyclodextrin complexes in solution. Chem. Rev. 1997, 97:1325-1358.
    • (1997) Chem. Rev. , vol.97 , pp. 1325-1358
    • Connors, K.A.1
  • 13
    • 0242319564 scopus 로고    scopus 로고
    • Toxic effects of brominated flame retardants in man and in wildlife
    • Darnerud P.O. Toxic effects of brominated flame retardants in man and in wildlife. Environ. Int. 2003, 29:841-853.
    • (2003) Environ. Int. , vol.29 , pp. 841-853
    • Darnerud, P.O.1
  • 14
    • 0032867556 scopus 로고    scopus 로고
    • The three recombinant domains of human serum albumin: structure characterization and ligand binding properties
    • Dockal M., Carter D.C., Ruker F. The three recombinant domains of human serum albumin: structure characterization and ligand binding properties. J. Biol. Chem. 1999, 274:29303-29310.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29303-29310
    • Dockal, M.1    Carter, D.C.2    Ruker, F.3
  • 15
    • 84868151520 scopus 로고    scopus 로고
    • EFSA panel on contaminants in the food chain (CONTAM), scientific opinion on tetrabromobisphenol A (TBBPA) and its derivatives in food
    • EFSA panel on contaminants in the food chain (CONTAM), scientific opinion on tetrabromobisphenol A (TBBPA) and its derivatives in food. EFSA J. 2011, 9:2477-2544.
    • (2011) EFSA J. , vol.9 , pp. 2477-2544
  • 16
    • 0019524375 scopus 로고
    • The location of drug binding sites in human serum albumin
    • Fehske K.J., Muller W.E., Wollert U. The location of drug binding sites in human serum albumin. Biochem. Pharmacol. 1981, 30:687-692.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 687-692
    • Fehske, K.J.1    Muller, W.E.2    Wollert, U.3
  • 17
    • 84862175886 scopus 로고    scopus 로고
    • Multispectroscopic and molecular modeling approach to investigate the interaction of flavokawain B with human serum albumin
    • Feroz S.R., Mohamad S.B., Bujang N., Malek S.N.A., Tayyab S. Multispectroscopic and molecular modeling approach to investigate the interaction of flavokawain B with human serum albumin. J. Agric. Food Chem. 2012, 60:5899-5908.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 5899-5908
    • Feroz, S.R.1    Mohamad, S.B.2    Bujang, N.3    Malek, S.N.A.4    Tayyab, S.5
  • 20
    • 41949122581 scopus 로고    scopus 로고
    • GM1-induced structural changes of bovine serum albumin after chemical and thermal disruption of the secondary structure: a spectroscopic comparison
    • Gayen A., Chatterjee C., Mukhopadhyay C. GM1-induced structural changes of bovine serum albumin after chemical and thermal disruption of the secondary structure: a spectroscopic comparison. Biomacromolecules 2008, 9:974-983.
    • (2008) Biomacromolecules , vol.9 , pp. 974-983
    • Gayen, A.1    Chatterjee, C.2    Mukhopadhyay, C.3
  • 22
    • 0025968147 scopus 로고
    • Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin
    • Hamilton J.A., Era S., Bhamidipati S.P., Reed R.G. Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:2051-2054.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2051-2054
    • Hamilton, J.A.1    Era, S.2    Bhamidipati, S.P.3    Reed, R.G.4
  • 23
    • 77951977658 scopus 로고    scopus 로고
    • Effects of repeated exposure to decabrominated diphenyl ether (BDE-209) on mice nervous system and its self
    • Liang S.X., Gao H.X., Zhao Y.Y., Ma X.M., Sun H.W. Effects of repeated exposure to decabrominated diphenyl ether (BDE-209) on mice nervous system and its self. Environ. Toxicol. Pharmacol. 2010, 29:297-301.
    • (2010) Environ. Toxicol. Pharmacol. , vol.29 , pp. 297-301
    • Liang, S.X.1    Gao, H.X.2    Zhao, Y.Y.3    Ma, X.M.4    Sun, H.W.5
  • 24
    • 84891473453 scopus 로고    scopus 로고
    • Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study
    • Li X., Wang G., Chen D., Lu Y. Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study. Mol. BioSyst. 2014, 10:326-337.
    • (2014) Mol. BioSyst. , vol.10 , pp. 326-337
    • Li, X.1    Wang, G.2    Chen, D.3    Lu, Y.4
  • 25
    • 78650271320 scopus 로고    scopus 로고
    • Fate of tetrabromobisphenol A and hexabromocyclododecane brominated flame retardants in soil and uptake by plants
    • Li Y., Zhou Q., Wang Y., Xie X. Fate of tetrabromobisphenol A and hexabromocyclododecane brominated flame retardants in soil and uptake by plants. Chemosphere 2011, 82:204-209.
    • (2011) Chemosphere , vol.82 , pp. 204-209
    • Li, Y.1    Zhou, Q.2    Wang, Y.3    Xie, X.4
  • 28
    • 84892631607 scopus 로고    scopus 로고
    • Interaction of procyanidin B3 with bovine serum albumin
    • Li X.R., Wang G.K., Chen D.J., Lu Y. Interaction of procyanidin B3 with bovine serum albumin. RSC Adv. 2014, 4:7301-7312.
    • (2014) RSC Adv. , vol.4 , pp. 7301-7312
    • Li, X.R.1    Wang, G.K.2    Chen, D.J.3    Lu, Y.4
  • 29
    • 51349131362 scopus 로고    scopus 로고
    • Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation
    • Nicoletti F.P., Howes B.D., Fittipaldi M., Fanali G., Fasano M., Ascenzi P., Smulevich G. Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation. J. Am. Chem. Soc. 2008, 130:11677-11688.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11677-11688
    • Nicoletti, F.P.1    Howes, B.D.2    Fittipaldi, M.3    Fanali, G.4    Fasano, M.5    Ascenzi, P.6    Smulevich, G.7
  • 30
    • 84862790974 scopus 로고    scopus 로고
    • The influence of Cd2+, Hg2+ and Pb2+ on taxifolin binding to bovine serum albumin by spectroscopy methods: with the viewpoint of toxic ions/drug interference
    • Peng M.J., Shi S.Y., Zhang Y.P. The influence of Cd2+, Hg2+ and Pb2+ on taxifolin binding to bovine serum albumin by spectroscopy methods: with the viewpoint of toxic ions/drug interference. Environ. Toxicol. Pharmacol. 2012, 33:327-333.
    • (2012) Environ. Toxicol. Pharmacol. , vol.33 , pp. 327-333
    • Peng, M.J.1    Shi, S.Y.2    Zhang, Y.P.3
  • 31
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross P.D., Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981, 20:3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 32
    • 84889673078 scopus 로고    scopus 로고
    • Molecular modeling and spectroscopic studies on the interaction of the chiral drug venlafaxine hydrochloride with bovine serum albumin
    • Shahabadi N., Hadidi S. Molecular modeling and spectroscopic studies on the interaction of the chiral drug venlafaxine hydrochloride with bovine serum albumin. Spectrachim. Acta Park A 2014, 122:100-106.
    • (2014) Spectrachim. Acta Park A , vol.122 , pp. 100-106
    • Shahabadi, N.1    Hadidi, S.2
  • 33
    • 84891440719 scopus 로고    scopus 로고
    • Multi-spectroscopic and molecular modeling studies on the interaction of antihypertensive drug; methyldopa with calf thymus DNA
    • Shahabadi N., Maghsudi M. Multi-spectroscopic and molecular modeling studies on the interaction of antihypertensive drug; methyldopa with calf thymus DNA. Mol. Biosyst. 2014, 10:338-347.
    • (2014) Mol. Biosyst. , vol.10 , pp. 338-347
    • Shahabadi, N.1    Maghsudi, M.2
  • 34
    • 0035476160 scopus 로고    scopus 로고
    • Brominated flame retardants in serum from U.S. blood donors
    • Sjödin A., Patterson D.G., Bergman A. Brominated flame retardants in serum from U.S. blood donors. Environ. Sci. Technol. 2001, 35:3830-3833.
    • (2001) Environ. Sci. Technol. , vol.35 , pp. 3830-3833
    • Sjödin, A.1    Patterson, D.G.2    Bergman, A.3
  • 36
    • 33846060214 scopus 로고    scopus 로고
    • Flame retardant tetrabromobusphenol A induced hepatic changes in ICR male mice
    • Tada Y., Fujitani T., Ogata A., Kamimura H. Flame retardant tetrabromobusphenol A induced hepatic changes in ICR male mice. Environ. Toxicol. Pharmacol. 2007, 23:174-178.
    • (2007) Environ. Toxicol. Pharmacol. , vol.23 , pp. 174-178
    • Tada, Y.1    Fujitani, T.2    Ogata, A.3    Kamimura, H.4
  • 37
    • 80054707450 scopus 로고    scopus 로고
    • Brominated flame retardants in the atmosphere of E-waste and rural sites in southern China: seasonal variation, temperature dependence, and gas-particle partitioning
    • Tian M., Chen S.J., Wang J., Zheng X.B., Luo X.J., Mai B.X. Brominated flame retardants in the atmosphere of E-waste and rural sites in southern China: seasonal variation, temperature dependence, and gas-particle partitioning. Environ. Sci. Technol. 2011, 45:8819-8825.
    • (2011) Environ. Sci. Technol. , vol.45 , pp. 8819-8825
    • Tian, M.1    Chen, S.J.2    Wang, J.3    Zheng, X.B.4    Luo, X.J.5    Mai, B.X.6
  • 38
    • 52949094558 scopus 로고    scopus 로고
    • Hydrolytic metal with a hydrophobic periphery: titanium (IV) complexes of naphthalene-2,3-diolate and interactions with serum albumin
    • Tinoco A.D., Eames E.V., Incarvito C.D., Valentine A.M. Hydrolytic metal with a hydrophobic periphery: titanium (IV) complexes of naphthalene-2,3-diolate and interactions with serum albumin. Inorg. Chem. 2008, 47:8380-8390.
    • (2008) Inorg. Chem. , vol.47 , pp. 8380-8390
    • Tinoco, A.D.1    Eames, E.V.2    Incarvito, C.D.3    Valentine, A.M.4
  • 39
    • 80053454439 scopus 로고    scopus 로고
    • Decabromodiphenyl ether (BDE-209) enters the food web of the River Po and is metabolically debrominated in resident cyprinid fishes
    • Viganò L., Roscioli C., Guzzella L. Decabromodiphenyl ether (BDE-209) enters the food web of the River Po and is metabolically debrominated in resident cyprinid fishes. Sci. Total Environ. 2011, 409:4966-4972.
    • (2011) Sci. Total Environ. , vol.409 , pp. 4966-4972
    • Viganò, L.1    Roscioli, C.2    Guzzella, L.3
  • 40
    • 84862263586 scopus 로고    scopus 로고
    • Interaction and nanotoxic effect of TiO2 nanoparticles on fibrinogen by multi-spectroscopic method
    • Wang C., Li Y. Interaction and nanotoxic effect of TiO2 nanoparticles on fibrinogen by multi-spectroscopic method. Sci. Total Environ. 2012, 429:156-160.
    • (2012) Sci. Total Environ. , vol.429 , pp. 156-160
    • Wang, C.1    Li, Y.2
  • 41
    • 60549102262 scopus 로고    scopus 로고
    • Studies on the interaction between imidacloprid and human serum albumin: spectroscopic approach
    • Wang Y.Q., Tang B.P., Zhang H.M., Zhou Q.H., Zhang G.C. Studies on the interaction between imidacloprid and human serum albumin: spectroscopic approach. J. Photochem. Photobiol. B: Biol. 2009, 94:183-190.
    • (2009) J. Photochem. Photobiol. B: Biol. , vol.94 , pp. 183-190
    • Wang, Y.Q.1    Tang, B.P.2    Zhang, H.M.3    Zhou, Q.H.4    Zhang, G.C.5
  • 42
    • 84862222406 scopus 로고    scopus 로고
    • Investigations on the binding of human hemoglobin with orange I and orange II
    • Wang Y.Q., Zhang H.M. Investigations on the binding of human hemoglobin with orange I and orange II. J. Photochem. Photobiol. B: Biol. 2012, 113:14-21.
    • (2012) J. Photochem. Photobiol. B: Biol. , vol.113 , pp. 14-21
    • Wang, Y.Q.1    Zhang, H.M.2
  • 43
    • 84889082908 scopus 로고    scopus 로고
    • Molecular interactions of benzophenone UV filters with human serum albumin revealed by spectroscopic techniques and molecular modeling
    • Zhang F., Zhang J., Tong C., Chen Y., Zhang S., Liu W. Molecular interactions of benzophenone UV filters with human serum albumin revealed by spectroscopic techniques and molecular modeling. J. Hazard Mater. 2013, 263:618-626.
    • (2013) J. Hazard Mater. , vol.263 , pp. 618-626
    • Zhang, F.1    Zhang, J.2    Tong, C.3    Chen, Y.4    Zhang, S.5    Liu, W.6
  • 44
    • 84863010203 scopus 로고    scopus 로고
    • Ecotoxicological effects of decabromodiphenyl ether and cadmium contamination on soil microbes and enzymes
    • Zhang W., Zhang M., An S., Xiong B., Li H., Cui C., Lin K. Ecotoxicological effects of decabromodiphenyl ether and cadmium contamination on soil microbes and enzymes. Ecotoxicol. Environ. Saf. 2012, 82:71-79.
    • (2012) Ecotoxicol. Environ. Saf. , vol.82 , pp. 71-79
    • Zhang, W.1    Zhang, M.2    An, S.3    Xiong, B.4    Li, H.5    Cui, C.6    Lin, K.7
  • 45
    • 84884527262 scopus 로고    scopus 로고
    • Circular Dichroism spectroscopic detection of ligand binding induced subdomain IB specific structure adjustment of human serum albumin
    • Zsila F. Circular Dichroism spectroscopic detection of ligand binding induced subdomain IB specific structure adjustment of human serum albumin. J. Phys. Chem. B 2013, 117:10798-10806.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 10798-10806
    • Zsila, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.