메뉴 건너뛰기




Volumn 153, Issue , 2015, Pages 463-472

Deciphering the inhibitory mechanism of genistein on xanthine oxidase in vitro

Author keywords

Competitive inhibitor; Genistein; Inhibition mechanism; Molecular simulation; Multispectroscopic methods; Xanthine oxidase

Indexed keywords

GENISTEIN; XANTHINE OXIDASE; ALLOPURINOL; ENZYME INHIBITOR; PROTEIN BINDING;

EID: 84946811740     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2015.10.022     Document Type: Article
Times cited : (42)

References (54)
  • 1
    • 33644631485 scopus 로고    scopus 로고
    • Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol
    • P. Pacher, A. Nivorozhkin, and C. Szabó Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol Pharmacol. Rev. 58 2006 87 114
    • (2006) Pharmacol. Rev. , vol.58 , pp. 87-114
    • Pacher, P.1    Nivorozhkin, A.2    Szabó, C.3
  • 2
    • 67649790241 scopus 로고    scopus 로고
    • Substrate orientation and catalysis at the molybdenum site in xanthine oxidase crystal structures in complex with xanthine and lumazine
    • J.M. Pauff, H. Cao, and R. Hille Substrate orientation and catalysis at the molybdenum site in xanthine oxidase crystal structures in complex with xanthine and lumazine J. Biol. Chem. 284 2009 8760 8767
    • (2009) J. Biol. Chem. , vol.284 , pp. 8760-8767
    • Pauff, J.M.1    Cao, H.2    Hille, R.3
  • 3
    • 84875143235 scopus 로고    scopus 로고
    • An electrochemical biosensor for the rapid detection of DNA damage induced by xanthine oxidase-catalyzed Fenton reaction
    • H. Xiong, Y. Chen, X. Zhang, H. Gu, and S. Wang An electrochemical biosensor for the rapid detection of DNA damage induced by xanthine oxidase-catalyzed Fenton reaction Sens. Actuators B 181 2013 85 91
    • (2013) Sens. Actuators B , vol.181 , pp. 85-91
    • Xiong, H.1    Chen, Y.2    Zhang, X.3    Gu, H.4    Wang, S.5
  • 4
    • 33947253955 scopus 로고    scopus 로고
    • Treatment with the xanthine oxidase inhibitor, allopurinol, improves nerve and vascular function in diabetic rats
    • M.E. Inkster, M.A. Cotter, and N.E. Cameron Treatment with the xanthine oxidase inhibitor, allopurinol, improves nerve and vascular function in diabetic rats Eur. J. Pharmacol. 561 2007 63 71
    • (2007) Eur. J. Pharmacol. , vol.561 , pp. 63-71
    • Inkster, M.E.1    Cotter, M.A.2    Cameron, N.E.3
  • 6
    • 0037449776 scopus 로고    scopus 로고
    • An extremely potent inhibitor of xanthine oxidoreductase crystal structure of the enzyme-inhibitor complex and mechanism of inhibition
    • K. Okamoto, B.T. Eger, T. Nishino, S. Kondo, E.F. Pai, and T. Nishino An extremely potent inhibitor of xanthine oxidoreductase crystal structure of the enzyme-inhibitor complex and mechanism of inhibition J. Biol. Chem. 278 2003 1848 1855
    • (2003) J. Biol. Chem. , vol.278 , pp. 1848-1855
    • Okamoto, K.1    Eger, B.T.2    Nishino, T.3    Kondo, S.4    Pai, E.F.5    Nishino, T.6
  • 9
    • 84872235042 scopus 로고    scopus 로고
    • Design and synthesis of Aza-flavones as a new class of xanthine oxidase inhibitors
    • R. Dhiman, S. Sharma, G. Singh, K. Nepali, and P.M.S. Bedi Design and synthesis of Aza-flavones as a new class of xanthine oxidase inhibitors Arch. Pharm. 346 2013 7 16
    • (2013) Arch. Pharm. , vol.346 , pp. 7-16
    • Dhiman, R.1    Sharma, S.2    Singh, G.3    Nepali, K.4    Bedi, P.M.S.5
  • 10
    • 84891861908 scopus 로고    scopus 로고
    • Microwave assisted synthesis of naphthopyrans catalysed by silica supported fluoroboric acid as a new class of non purine xanthine oxidase inhibitors
    • S. Sharma, K. Sharma, R. Ojha, D. Kumar, G. Singh, K. Nepali, and P.M.S. Bedi Microwave assisted synthesis of naphthopyrans catalysed by silica supported fluoroboric acid as a new class of non purine xanthine oxidase inhibitors Bioorg. Med. Chem. Lett. 24 2014 495 500
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 495-500
    • Sharma, S.1    Sharma, K.2    Ojha, R.3    Kumar, D.4    Singh, G.5    Nepali, K.6    Bedi, P.M.S.7
  • 11
    • 84906935070 scopus 로고    scopus 로고
    • Synthesis and evaluation of naphthoflavones as a new class of non purine xanthine oxidase inhibitors
    • H. Singh, S. Sharma, R. Ojha, M.K. Gupta, K. Nepali, and P.M.S. Bedi Synthesis and evaluation of naphthoflavones as a new class of non purine xanthine oxidase inhibitors Bioorg. Med. Chem. Lett. 24 2014 4192 4197
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 4192-4197
    • Singh, H.1    Sharma, S.2    Ojha, R.3    Gupta, M.K.4    Nepali, K.5    Bedi, P.M.S.6
  • 12
    • 79551506506 scopus 로고    scopus 로고
    • Inhibition of xanthine oxidase activity by an oxathiolanone derivative of quercetin
    • U. Takahama, Y. Koga, S. Hirota, and R. Yamauchi Inhibition of xanthine oxidase activity by an oxathiolanone derivative of quercetin Food Chem. 126 2011 1808 1811
    • (2011) Food Chem. , vol.126 , pp. 1808-1811
    • Takahama, U.1    Koga, Y.2    Hirota, S.3    Yamauchi, R.4
  • 13
    • 65649103461 scopus 로고    scopus 로고
    • Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin
    • J.M. Pauff, and R. Hille Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin J. Nat. Prod. 72 2009 725 731
    • (2009) J. Nat. Prod. , vol.72 , pp. 725-731
    • Pauff, J.M.1    Hille, R.2
  • 19
    • 0035854819 scopus 로고    scopus 로고
    • Genistein, a soy isoflavone, is a potent α-glucosidase inhibitor
    • D.S. Lee, and S.H. Lee Genistein, a soy isoflavone, is a potent α-glucosidase inhibitor FEBS Lett. 501 2001 84 86
    • (2001) FEBS Lett. , vol.501 , pp. 84-86
    • Lee, D.S.1    Lee, S.H.2
  • 22
    • 0036256859 scopus 로고    scopus 로고
    • Prevention of cellular ROS damage by isovitexin and related flavonoids
    • C.M. Lin, C.T. Chen, H.H. Lee, and J.K. Lin Prevention of cellular ROS damage by isovitexin and related flavonoids Planta Med. 68 2002 365 367
    • (2002) Planta Med. , vol.68 , pp. 365-367
    • Lin, C.M.1    Chen, C.T.2    Lee, H.H.3    Lin, J.K.4
  • 23
    • 84921514007 scopus 로고    scopus 로고
    • Novel insights into the inhibitory mechanism of kaempferol on xanthine oxidase
    • Y.J. Wang, G.W. Zhang, J.H. Pan, and D.M. Gong Novel insights into the inhibitory mechanism of kaempferol on xanthine oxidase J. Agric. Food Chem. 63 2015 526 534
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 526-534
    • Wang, Y.J.1    Zhang, G.W.2    Pan, J.H.3    Gong, D.M.4
  • 25
    • 84897119743 scopus 로고    scopus 로고
    • Effect of luteolin on xanthine oxidase: Inhibition kinetics and interaction mechanism merging with docking simulation
    • J.K. Yan, G.W. Zhang, Y.T. Hu, and Y.D. Ma Effect of luteolin on xanthine oxidase: Inhibition kinetics and interaction mechanism merging with docking simulation Food Chem. 141 2013 3766 3773
    • (2013) Food Chem. , vol.141 , pp. 3766-3773
    • Yan, J.K.1    Zhang, G.W.2    Hu, Y.T.3    Ma, Y.D.4
  • 26
    • 84860615530 scopus 로고    scopus 로고
    • Spectroscopic study on the interaction of eugenol with salmon sperm DNA in vitro
    • S. Bi, L. Yan, Y. Wang, B. Pang, and T. Wang Spectroscopic study on the interaction of eugenol with salmon sperm DNA in vitro J. Lumin. 132 2012 2355 2360
    • (2012) J. Lumin. , vol.132 , pp. 2355-2360
    • Bi, S.1    Yan, L.2    Wang, Y.3    Pang, B.4    Wang, T.5
  • 27
    • 84890843811 scopus 로고    scopus 로고
    • Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis
    • C. Hebia, L. Bekale, P. Chanphai, J. Agbebavi, and H.A. Tajmir-Riahi Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis J. Photochem. Photobiol. B 130 2014 254 259
    • (2014) J. Photochem. Photobiol. B , vol.130 , pp. 254-259
    • Hebia, C.1    Bekale, L.2    Chanphai, P.3    Agbebavi, J.4    Tajmir-Riahi, H.A.5
  • 28
    • 79959242562 scopus 로고    scopus 로고
    • characterizing the interaction between tartrazine and two serum albumins by a hybrid spectroscopic approach
    • X. Pan, and P. Qin R Liu, J. Wang, characterizing the interaction between tartrazine and two serum albumins by a hybrid spectroscopic approach J. Agric. Food Chem. 59 2011 6650 6656
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 6650-6656
    • Pan, X.1    Qin, P.2    Liu, R.3    Wang, J.4
  • 29
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • T. Nishino, K. Okamoto, B.T. Eger, E.F. Pai, and T. Nishino Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase FEBS J. 275 2008 3278 3289
    • (2008) FEBS J. , vol.275 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 33
    • 84901660524 scopus 로고    scopus 로고
    • Evaluation of the biointeraction of colorant flavazin with human serum albumin: insights from multiple spectroscopic studies, in silico docking and molecular dynamics simulation
    • W. Peng, F. Ding, Y.T. Jiang, Y. Sun, and Y.K. Peng Evaluation of the biointeraction of colorant flavazin with human serum albumin: insights from multiple spectroscopic studies, in silico docking and molecular dynamics simulation Food Funct. 5 2014 1203 1217
    • (2014) Food Funct. , vol.5 , pp. 1203-1217
    • Peng, W.1    Ding, F.2    Jiang, Y.T.3    Sun, Y.4    Peng, Y.K.5
  • 34
    • 84891473453 scopus 로고    scopus 로고
    • Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study
    • X. Li, G. Wang, D. Chen, and Y. Lu Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study Mol. BioSyst. 10 2014 326 337
    • (2014) Mol. BioSyst. , vol.10 , pp. 326-337
    • Li, X.1    Wang, G.2    Chen, D.3    Lu, Y.4
  • 35
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • J.R. Lakowicz, and G. Weber Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules Biochemistry 12 1973 4161 4170
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 36
    • 84866066209 scopus 로고    scopus 로고
    • Spectroscopic investigations on the interactions of potent platinum (II) anticancer agents with bovine serum albumin
    • A.M. Krause-Heuer, W.S. Price, and J.R. Aldrich-Wright Spectroscopic investigations on the interactions of potent platinum (II) anticancer agents with bovine serum albumin J. Chem. Biol. 5 2012 105 113
    • (2012) J. Chem. Biol. , vol.5 , pp. 105-113
    • Krause-Heuer, A.M.1    Price, W.S.2    Aldrich-Wright, J.R.3
  • 37
    • 73449122218 scopus 로고    scopus 로고
    • Spectroscopic investigations of pentobarbital interaction with human serum albumin
    • S.M. Darwish, M.M. Abu Teir, S.A. Makharza, and M.M. Abu-hadid Spectroscopic investigations of pentobarbital interaction with human serum albumin J. Mol. Struct. 963 2010 122 129
    • (2010) J. Mol. Struct. , vol.963 , pp. 122-129
    • Darwish, S.M.1    Abu Teir, M.M.2    Makharza, S.A.3    Abu-Hadid, M.M.4
  • 38
    • 27844526058 scopus 로고    scopus 로고
    • Studies on the interaction of colloidal gold and serum albumins by spectral methods
    • D. Gao, Y. Tian, S. Bi, Y. Chen, A. Yu, and H. Zhang Studies on the interaction of colloidal gold and serum albumins by spectral methods Spectrochim Acta, Part A 62 2005 1203 1208
    • (2005) Spectrochim Acta, Part A , vol.62 , pp. 1203-1208
    • Gao, D.1    Tian, Y.2    Bi, S.3    Chen, Y.4    Yu, A.5    Zhang, H.6
  • 40
    • 79952317427 scopus 로고    scopus 로고
    • Application of molecular modelling and spectroscopic approaches for investigating binding of vanillin to human serum albumin
    • X. Wang, X. Xie, C. Ren, Y. Yang, X. Xu, and X. Chen Application of molecular modelling and spectroscopic approaches for investigating binding of vanillin to human serum albumin Food Chem. 127 2011 705 710
    • (2011) Food Chem. , vol.127 , pp. 705-710
    • Wang, X.1    Xie, X.2    Ren, C.3    Yang, Y.4    Xu, X.5    Chen, X.6
  • 41
    • 14744268162 scopus 로고    scopus 로고
    • Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin
    • 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
    • (2005) J. Mol. Struct. , vol.738 , pp. 143-147
    • Hu, Y.J.1    Liu, Y.2    Shen, X.S.3    Fang, X.Y.4    Qu, S.S.5
  • 42
    • 65249134878 scopus 로고    scopus 로고
    • Investigation of the interaction between berberine and human serum albumin
    • Y.J. Hu, Y. Liu, and X.H. Xiao Investigation of the interaction between berberine and human serum albumin Biomacromolecules 10 2009 517 521
    • (2009) Biomacromolecules , vol.10 , pp. 517-521
    • Hu, Y.J.1    Liu, Y.2    Xiao, X.H.3
  • 43
    • 84870007663 scopus 로고    scopus 로고
    • Probing the adverse temperature dependence in the static fluorescence quenching of BSA induced by a novel anticancer hydrazone
    • J.Q. Tong, F.F. Tian, Q. Li, L.L. Li, C. Xiang, Y. Liu, J. Dai, and F.L. Jiang Probing the adverse temperature dependence in the static fluorescence quenching of BSA induced by a novel anticancer hydrazone Photochem. Photobiol. Sci. 11 2012 1868 1879
    • (2012) Photochem. Photobiol. Sci. , vol.11 , pp. 1868-1879
    • Tong, J.Q.1    Tian, F.F.2    Li, Q.3    Li, L.L.4    Xiang, C.5    Liu, Y.6    Dai, J.7    Jiang, F.L.8
  • 44
    • 55949121032 scopus 로고    scopus 로고
    • Interaction of mitoxantrone with human serum albumin: spectroscopic and molecular modeling studies
    • S.N. Khan, B. Islam, R. Yennamalli, A. Sultan, N. Subbarao, and A.U. Khan Interaction of mitoxantrone with human serum albumin: spectroscopic and molecular modeling studies Eur. J. Pharm. Sci. 35 2008 371 382
    • (2008) Eur. J. Pharm. Sci. , vol.35 , pp. 371-382
    • Khan, S.N.1    Islam, B.2    Yennamalli, R.3    Sultan, A.4    Subbarao, N.5    Khan, A.U.6
  • 45
    • 84882805113 scopus 로고    scopus 로고
    • Study on the interaction of the drug mesalamine with calf thymus DNA using molecular docking and spectroscopic techniques
    • N. Shahabadi, S.M. Fili, and F. Kheirdoosh Study on the interaction of the drug mesalamine with calf thymus DNA using molecular docking and spectroscopic techniques J. Photochem. Photobiol. B 128 2013 20 26
    • (2013) J. Photochem. Photobiol. B , vol.128 , pp. 20-26
    • Shahabadi, N.1    Fili, S.M.2    Kheirdoosh, F.3
  • 46
    • 84863362068 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques
    • G.W. Zhang, L.H. 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.H.2    Pan, J.H.3
  • 47
    • 84862175886 scopus 로고    scopus 로고
    • Multispectroscopic and molecular modeling approach to investigate the interaction of flavokawain B with human serum albumin
    • S.R. Feroz, S.B. Mohamad, N. Bujang, S.N. Malek, and S. Tayyab Multispectroscopic and molecular modeling approach to investigate the interaction of flavokawain B with human serum albumin J. Agric. Food Chem. 60 2012 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.4    Tayyab, S.5
  • 48
    • 84859431870 scopus 로고    scopus 로고
    • Formation of molten globule-like state during acid denaturation of Aspergillus niger glucoamylase
    • M.S. Zaroog, and S. Tayyab Formation of molten globule-like state during acid denaturation of Aspergillus niger glucoamylase Process Biochem. 47 2012 775 784
    • (2012) Process Biochem. , vol.47 , pp. 775-784
    • Zaroog, M.S.1    Tayyab, S.2
  • 49
    • 84872594809 scopus 로고    scopus 로고
    • Study of the interaction of deoxynivalenol with human serum albumin by spectroscopic technique and molecular modelling
    • Y. Li, H. Wang, B. Jia, C. Liu, K. Liu, Y. Qi, and Z. Hu Study of the interaction of deoxynivalenol with human serum albumin by spectroscopic technique and molecular modelling Food Addit. Contam. A 30 2013 356 364
    • (2013) Food Addit. Contam. A , vol.30 , pp. 356-364
    • Li, Y.1    Wang, H.2    Jia, B.3    Liu, C.4    Liu, K.5    Qi, Y.6    Hu, Z.7
  • 50
    • 84862134774 scopus 로고    scopus 로고
    • Combined fluorescence spectroscopy and molecular modeling studies on the interaction between harmalol and human serum albumin
    • B. Hemmateenejad, M. Shamsipur, F. Samari, T. Khayamian, M. Ebrahimi, and Z. Rezaei Combined fluorescence spectroscopy and molecular modeling studies on the interaction between harmalol and human serum albumin J. Pharm. Biomed. Anal. 67 2012 201 208
    • (2012) J. Pharm. Biomed. Anal. , vol.67 , pp. 201-208
    • Hemmateenejad, B.1    Shamsipur, M.2    Samari, F.3    Khayamian, T.4    Ebrahimi, M.5    Rezaei, Z.6
  • 51
    • 61949432567 scopus 로고    scopus 로고
    • Structural analysis of human serum albumin complexes with cationic lipids
    • D. Charbonneau, M. Beauregard, and H.A. Tajmir-Riahi Structural analysis of human serum albumin complexes with cationic lipids J. Phys. Chem. B 113 2009 1777 1784
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1777-1784
    • Charbonneau, D.1    Beauregard, M.2    Tajmir-Riahi, H.A.3
  • 52
    • 77954756913 scopus 로고    scopus 로고
    • Interaction between a potent corticosteroid drug-dexamethasone with bovine serum albumin and human serum albumin: a fluorescence quenching and Fourier transformation infrared spectroscopy study
    • P.N. Naik, S.A. Chimatadar, and S.T. Nandibewoor Interaction between a potent corticosteroid drug-dexamethasone with bovine serum albumin and human serum albumin: a fluorescence quenching and Fourier transformation infrared spectroscopy study J. Photochem. Photobiol. B 100 2010 147 159
    • (2010) J. Photochem. Photobiol. B , vol.100 , pp. 147-159
    • Naik, P.N.1    Chimatadar, S.A.2    Nandibewoor, S.T.3
  • 53
    • 79952278667 scopus 로고    scopus 로고
    • Biological relevance of the interaction between procyanidins and trypsin: a multitechnique approach
    • R. Gonçalves, N. Mateus, and V. De Freitas Biological relevance of the interaction between procyanidins and trypsin: a multitechnique approach J. Agric. Food Chem. 58 2010 11924 11931
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 11924-11931
    • Gonçalves, R.1    Mateus, N.2    De Freitas, V.3
  • 54
    • 79953747269 scopus 로고    scopus 로고
    • Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin
    • M. Hossain, A.Y. Khan, and G.S. Kumar Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin PLoS One 6 2011 e18333
    • (2011) PLoS One , vol.6
    • Hossain, M.1    Khan, A.Y.2    Kumar, G.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.