메뉴 건너뛰기




Volumn 138, Issue , 2014, Pages 182-190

Binding of a new bisphenol analogue, bisphenol S to bovine serum albumin and calf thymus DNA

Author keywords

Binding mode; Bisphenol S; Bovine serum albumin; DNA; Molecular modeling

Indexed keywords

4,4' ISOPROPYLIDENEDIPHENOL; BISPHENOL S; BOVINE SERUM ALBUMIN; CALF THYMUS DNA; DNA; PHENOL DERIVATIVE; UNCLASSIFIED DRUG; BIS(4-HYDROXYPHENYL)SULFONE; PROTEIN BINDING; SULFONE;

EID: 84903267508     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2014.06.002     Document Type: Article
Times cited : (37)

References (43)
  • 2
    • 84862524447 scopus 로고    scopus 로고
    • Bisphenol S, a new bisphenol analogue, in paper products and currency bills and its association with bisphenol a residues
    • C. Liao, F. Liu, and K. Kannan Bisphenol S, a new bisphenol analogue, in paper products and currency bills and its association with bisphenol a residues Environ. Sci. Technol. 46 2012 6515 6522
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 6515-6522
    • Liao, C.1    Liu, F.2    Kannan, K.3
  • 3
    • 84874624091 scopus 로고    scopus 로고
    • Bisphenol S disrupts estradiol-induced nongenomic signalling in a rat pituitary cell line: Effects on cell functions
    • R. Viñas, and C.S. Watson Bisphenol S disrupts estradiol-induced nongenomic signalling in a rat pituitary cell line: effects on cell functions Environ. Health Perspect. 121 2013 352 358
    • (2013) Environ. Health Perspect. , vol.121 , pp. 352-358
    • Viñas, R.1    Watson, C.S.2
  • 4
    • 84881420196 scopus 로고    scopus 로고
    • Effects of bisphenol S exposure on endocrine functions and reproduction of zebrafish
    • K. Ji, S. Hong, Y. Kho, and K. Choi Effects of bisphenol S exposure on endocrine functions and reproduction of zebrafish Environ. Sci. Technol. 47 2013 8793 8800
    • (2013) Environ. Sci. Technol. , vol.47 , pp. 8793-8800
    • Ji, K.1    Hong, S.2    Kho, Y.3    Choi, K.4
  • 6
    • 77955175745 scopus 로고    scopus 로고
    • Investigation of the interaction between endocrine disruptor bisphenol A and human serum albumin
    • X. Xie, X. Wang, X. Xu, H. Sun, and X. Chen Investigation of the interaction between endocrine disruptor bisphenol A and human serum albumin Chemosphere 80 2010 1075 1080
    • (2010) Chemosphere , vol.80 , pp. 1075-1080
    • Xie, X.1    Wang, X.2    Xu, X.3    Sun, H.4    Chen, X.5
  • 7
    • 84898425233 scopus 로고    scopus 로고
    • Exploring the interaction of bisphenol-S with serum albumins: A better or worse alternative for bisphenol A?
    • M. Mathew, S. Sreedhanya, P. Manoj, C.T. Aravindakumar, and U.K. Aravind Exploring the interaction of bisphenol-S with serum albumins: a better or worse alternative for bisphenol A? J. Phys. Chem. B 118 2014 3832 3848
    • (2014) J. Phys. Chem. B , vol.118 , pp. 3832-3848
    • Mathew, M.1    Sreedhanya, S.2    Manoj, P.3    Aravindakumar, C.T.4    Aravind, U.K.5
  • 8
    • 77955571914 scopus 로고    scopus 로고
    • Binding of bisphenol A and acrylamide to BSA and DNA: Insights into the comparative interactions of harmful chemicals with functional biomacromolecules
    • Y.L. Zhang, X. Zhang, X.C. Fei, S.L. Wang, and H.W. Gao Binding of bisphenol A and acrylamide to BSA and DNA: insights into the comparative interactions of harmful chemicals with functional biomacromolecules J. Hazard. Mater. 182 2010 877 885
    • (2010) J. Hazard. Mater. , vol.182 , pp. 877-885
    • Zhang, Y.L.1    Zhang, X.2    Fei, X.C.3    Wang, S.L.4    Gao, H.W.5
  • 10
    • 79953288933 scopus 로고    scopus 로고
    • Spectroscopic study on interaction between bisphenol A or its degraded solution under microwave irradiation in the presence of activated carbon and human serum albumin
    • Z. Zhang, D. Xu, M. Tie, F. Li, Z. Chen, J. Wang, W. Gao, X. Ji, and Y. Xu Spectroscopic study on interaction between bisphenol A or its degraded solution under microwave irradiation in the presence of activated carbon and human serum albumin J. Lumin. 131 2011 1386 1392
    • (2011) J. Lumin. , vol.131 , pp. 1386-1392
    • Zhang, Z.1    Xu, D.2    Tie, M.3    Li, F.4    Chen, Z.5    Wang, J.6    Gao, W.7    Ji, X.8    Xu, Y.9
  • 11
    • 84899717125 scopus 로고    scopus 로고
    • Role of the flavan-3-ol and galloyl moieties in the interaction of (-)-epigallocatechin gallate with serum albumin
    • M. Li, and A.E. Hagerman Role of the flavan-3-ol and galloyl moieties in the interaction of (-)-epigallocatechin gallate with serum albumin J. Agric. Food Chem. 62 2014 3768 3775
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 3768-3775
    • Li, M.1    Hagerman, A.E.2
  • 12
    • 84892631607 scopus 로고    scopus 로고
    • Interaction of procyanidin B3 with bovine serum albumin
    • X.R. Li, G.K. Wang, D.J. Chen, and Y. Lu Interaction of procyanidin B3 with bovine serum albumin RSC Adv. 4 2014 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
  • 14
    • 84884212050 scopus 로고    scopus 로고
    • Spectroscopic studies of the effects of anticancer drug mitoxantrone interaction with calf-thymus DNA
    • S. Agarwal, D.K. Jangir, and R. Mehrotra Spectroscopic studies of the effects of anticancer drug mitoxantrone interaction with calf-thymus DNA J. Photochem. Photobiol. B 120 2013 177 182
    • (2013) J. Photochem. Photobiol. B , vol.120 , pp. 177-182
    • Agarwal, S.1    Jangir, D.K.2    Mehrotra, R.3
  • 15
    • 84862830153 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between carbaryl and calf thymus DNA with the use of ethidium bromide as a fluorescence probe
    • G.W. Zhang, X. Hu, and P. Fu Spectroscopic studies on the interaction between carbaryl and calf thymus DNA with the use of ethidium bromide as a fluorescence probe J. Photochem. Photobiol. B 108 2012 3 61
    • (2012) J. Photochem. Photobiol. B , vol.108 , pp. 3-61
    • Zhang, G.W.1    Hu, X.2    Fu, P.3
  • 16
    • 34347352255 scopus 로고    scopus 로고
    • Binding of the Environmental pollutant naphthol to bovine serum albumin
    • DOI 10.1021/bm061189v
    • T.Q. Wu, Q. Wu, S.Y. Guan, H.X. Su, and Z.J. Cai Binding of the environmental pollutant naphthol to bovine serum albumin Biomacromolecules 8 2007 1899 1906 (Pubitemid 47009969)
    • (2007) Biomacromolecules , vol.8 , Issue.6 , pp. 1899-1906
    • Wu, T.1    Wu, Q.2    Guan, S.3    Su, H.4    Cai, Z.5
  • 17
    • 33947455249 scopus 로고
    • A further examination of the molecular weight and size of desoxypentose nucleic acid
    • M.E. Reichmann, S.A. Rice, C.A. Thomas, and P. Doty A further examination of the molecular weight and size of desoxypentose nucleic acid J. Am. Chem. Soc. 76 1954 3047 3053
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 3047-3053
    • Reichmann, M.E.1    Rice, S.A.2    Thomas, C.A.3    Doty, P.4
  • 19
    • 84890018559 scopus 로고    scopus 로고
    • In vitro DNA binding studies of the sweetening agent saccharin and its copper(II) and zinc(II) complexes
    • C. Icsel, and V.T. Yilmaz In vitro DNA binding studies of the sweetening agent saccharin and its copper(II) and zinc(II) complexes J. Photochem. Photobiol. B: Biology 130 2014 115 121
    • (2014) J. Photochem. Photobiol. B: Biology , vol.130 , pp. 115-121
    • Icsel, C.1    Yilmaz, V.T.2
  • 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
    • DOI 10.1021/bm701144k
    • A. Gayen, C. Chatterjee, and C. Mukhopadhyay GM1-induced structural changes of bovine serum albumin after chemical and thermal disruption of the secondary structure: a spectroscopic comparison Biomacromolecules 9 2008 974 983 (Pubitemid 351560491)
    • (2008) Biomacromolecules , vol.9 , Issue.3 , pp. 974-983
    • Gayen, A.1    Chatterjee, C.2    Mukhopadhyay, C.3
  • 21
    • 84903294242 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb/explore.do?structureId=3V03.
  • 22
    • 84903294243 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb/explore/explore.do?structureId=1BNA.
  • 24
    • 84903294231 scopus 로고    scopus 로고
    • http://www.clcbio.com/products/molegro/.
  • 26
    • 84862222406 scopus 로고    scopus 로고
    • Investigations on the binding of human hemoglobin with orange i and orange
    • Y.Q. Wang, and H.M. Zhang Investigations on the binding of human hemoglobin with orange I and orange J. Photochem. Photobiol. B: Biol. 113 2012 14 21
    • (2012) J. Photochem. Photobiol. B: Biol. , vol.113 , pp. 14-21
    • Wang, Y.Q.1    Zhang, H.M.2
  • 27
    • 60549102262 scopus 로고    scopus 로고
    • Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach
    • Y.Q. Wang, B.P. Tang, H.M. Zhang, Q.H. Zhou, and G.C. Zhang Studies on the interaction between imidacloprid and human serum albumin: spectroscopic approach J. Photochem. Photobiol. B: Biol. 94 2009 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
  • 29
    • 84877074214 scopus 로고    scopus 로고
    • Drug-DNA interactions and their study by UV-Visible, fluorescence spectroscopies and cyclic voltametry
    • M. Sirajuddin, S. Ali, and A. Badshah Drug-DNA interactions and their study by UV-Visible, fluorescence spectroscopies and cyclic voltametry J. Photochem. Photobiol. B: Biol. 124 2013 1 19
    • (2013) J. Photochem. Photobiol. B: Biol. , vol.124 , pp. 1-19
    • Sirajuddin, M.1    Ali, S.2    Badshah, A.3
  • 30
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, and D.N. Wade The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 11 1975 824 832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 31
    • 84877265704 scopus 로고    scopus 로고
    • Subdomain IB is the third major drug binding region of human serum albumin: Toward the three-sites model
    • F. Zsila Subdomain IB is the third major drug binding region of human serum albumin: toward the three-sites model Mol. Pharmacol. 10 2013 1668 1682
    • (2013) Mol. Pharmacol. , vol.10 , pp. 1668-1682
    • Zsila, F.1
  • 32
    • 7744232695 scopus 로고    scopus 로고
    • Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket
    • DOI 10.1021/ja046022t
    • T. Komatsu, N. Ohmichi, P.A. Zunszain, S. Curry, and E. Tsuchida Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket J. Am. Chem. Soc. 126 2004 14304 14305 (Pubitemid 39463585)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.44 , pp. 14304-14305
    • Komatsu, T.1    Ohmichi, N.2    Zunszain, P.A.3    Curry, S.4    Tsuchida, E.5
  • 34
    • 62549142223 scopus 로고    scopus 로고
    • A fluorometric study of the interaction of C.I. Solvent red 24 with haemoglobin
    • H.M. Zhang, Y.Q. Wang, and M.L. Jiang A fluorometric study of the interaction of C.I. solvent red 24 with haemoglobin Dyes Pigm. 82 2009 156 163
    • (2009) Dyes Pigm. , vol.82 , pp. 156-163
    • Zhang, H.M.1    Wang, Y.Q.2    Jiang, M.L.3
  • 35
    • 0027249523 scopus 로고
    • The binding interaction of Coomassie blue with proteins
    • W.C. Abert, W.M. Gregory, and G.S. Allan The binding interaction of Coomassie blue with proteins Anal. Biochem. 213 1993 407 413
    • (1993) Anal. Biochem. , vol.213 , pp. 407-413
    • Abert, W.C.1    Gregory, W.M.2    Allan, G.S.3
  • 36
    • 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
    • F.P. Nicoletti, B.D. Howes, M. Fittipaldi, G. Fanali, M. Fasano, P. Ascenzi, and G. Smulevich Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation J. Am. Chem. Soc. 130 2008 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
  • 37
    • 84891440719 scopus 로고    scopus 로고
    • Multi-spectroscopic and molecular modeling studies on the interaction of antihypertensive drug; Methyldopa with calf thymus DNA
    • N. Shahabadi, and M. Maghsudi Multi-spectroscopic and molecular modeling studies on the interaction of antihypertensive drug; methyldopa with calf thymus DNA Mol. BioSyst. 10 2014 338 347
    • (2014) Mol. BioSyst. , vol.10 , pp. 338-347
    • Shahabadi, N.1    Maghsudi, M.2
  • 38
    • 84893447570 scopus 로고    scopus 로고
    • Exploring the biophysical aspects and binding mechanism of thionine with bovine hemoglobin by optical spectroscopic and molecular docking methods
    • K. Shanmugaraj, S. Anandakumar, and M. Ilanchelian Exploring the biophysical aspects and binding mechanism of thionine with bovine hemoglobin by optical spectroscopic and molecular docking methods J. Photochem. Photobiol. B: Biol. 131 2014 43 52
    • (2014) J. Photochem. Photobiol. B: Biol. , vol.131 , pp. 43-52
    • Shanmugaraj, K.1    Anandakumar, S.2    Ilanchelian, M.3
  • 39
    • 84894551704 scopus 로고    scopus 로고
    • Phenazinium dyes safranine O and phenosafranine induce self-structure in single stranded polyadenylic acid: Structural and thermodynamic studies
    • A.Y. Khan, B. Saha, and G.S. Kumar Phenazinium dyes safranine O and phenosafranine induce self-structure in single stranded polyadenylic acid: Structural and thermodynamic studies J. Photochem. Photobiol. B: Biol. 132 2014 17 26
    • (2014) J. Photochem. Photobiol. B: Biol. , vol.132 , pp. 17-26
    • Khan, A.Y.1    Saha, B.2    Kumar, G.S.3
  • 41
    • 78651291244 scopus 로고    scopus 로고
    • Phenotypic characterization of the binding of tetracycline to human serum albumin
    • Z.X. Chi, and R.T. Liu Phenotypic characterization of the binding of tetracycline to human serum albumin Biomacromolecules 12 2011 203 209
    • (2011) Biomacromolecules , vol.12 , pp. 203-209
    • Chi, Z.X.1    Liu, R.T.2
  • 42
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 1981 3096 3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 43
    • 84863362068 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques
    • G.W. Zhang, L. Wang, and J.H. Pan Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques J. Agric. Food Chem. 60 2012 2721 2729
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 2721-2729
    • Zhang, G.W.1    Wang, L.2    Pan, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.