메뉴 건너뛰기




Volumn 5, Issue 1, 2010, Pages

Molecular interaction studies of trimethoxy flavone with human serum albumin

Author keywords

[No Author keywords available]

Indexed keywords

FLAVONE; SERUM ALBUMIN; TRIMETHOXY FLAVONE; UNCLASSIFIED DRUG;

EID: 77749317543     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0008834     Document Type: Article
Times cited : (105)

References (57)
  • 1
    • 0034928799 scopus 로고    scopus 로고
    • Inhibition of carcinogenesis by dietary polyphenolic compounds
    • Yang CS, Landau JM, Huang HMT (2001) Inhibition of carcinogenesis by dietary polyphenolic compounds. Annu Rev Nutr 21: 381-406.
    • (2001) Annu Rev Nutr , vol.21 , pp. 381-406
    • Yang, C.S.1    Landau, J.M.2    Huang, H.M.T.3
  • 3
    • 0033637140 scopus 로고    scopus 로고
    • The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
    • Middleton E, Kandaswami C, Theoharides TC (2000) The effects of plant flavonoids on mammalian cells: implications for inflammation, heart disease, and cancer. Pharmacol Rev 52: 673-751.
    • (2000) Pharmacol Rev , vol.52 , pp. 673-751
    • Middleton, E.1    Kandaswami, C.2    Theoharides, T.C.3
  • 5
    • 0009538299 scopus 로고
    • Hydroxyl radical scavenging activity of flavonoids
    • Husain SR, Cillard J, Cillard P (1987) Hydroxyl radical scavenging activity of flavonoids. Phytochemistry 26: 2489-2491.
    • (1987) Phytochemistry , vol.26 , pp. 2489-2491
    • Husain, S.R.1    Cillard, J.2    Cillard, P.3
  • 6
    • 0037480882 scopus 로고    scopus 로고
    • Naringin, a citrus flavonone, protects against radiation-induced chromosome damage in mouse bone marrow
    • Jagetia GC, Venkatesha VA, Reddy TK (2003) Naringin, a citrus flavonone, protects against radiation-induced chromosome damage in mouse bone marrow. Mutagenesis 18: 337-343.
    • (2003) Mutagenesis , vol.18 , pp. 337-343
    • Jagetia, G.C.1    Venkatesha, V.A.2    Reddy, T.K.3
  • 7
    • 0035868671 scopus 로고    scopus 로고
    • Enhancement of antioxidant and anti-inflammatory activities of bioflavonoid rutin by complexation with transition metals
    • Afanaseva IB, Ostrakhovitch EA, Mikhalchik EV, Ibragimova GA, Korkina LG (2001) Enhancement of antioxidant and anti-inflammatory activities of bioflavonoid rutin by complexation with transition metals. Biochem pharmacol 61: 677-684.
    • (2001) Biochem pharmacol , vol.61 , pp. 677-684
    • Afanaseva, I.B.1    Ostrakhovitch, E.A.2    Mikhalchik, E.V.3    Ibragimova, G.A.4    Korkina, L.G.5
  • 8
    • 0022249093 scopus 로고
    • Inhibition of phosphorylase kinase, and tyrosine protein kinase activities by quercetin
    • Srivastava AK (1985) Inhibition of phosphorylase kinase, and tyrosine protein kinase activities by quercetin. Biochem Biophys Res Commun 131: 1-5.
    • (1985) Biochem Biophys Res Commun , vol.131 , pp. 1-5
    • Srivastava, A.K.1
  • 9
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos CJ, Matter WF, Hui KY, Brown RF (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J Biol Chem 269: 5241-5248.
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 10
    • 0030031184 scopus 로고    scopus 로고
    • Selected novel flavones inhibit the DNA binding or the DNA religation step of eukaryotic topoisomerase I
    • Boege F, Straub T, Kehr A, Boesenberg C, Christiansen K, et al. (1996) Selected novel flavones inhibit the DNA binding or the DNA religation step of eukaryotic topoisomerase I. J Biol Chem 271: 2262-2270.
    • (1996) J Biol Chem , vol.271 , pp. 2262-2270
    • Boege, F.1    Straub, T.2    Kehr, A.3    Boesenberg, C.4    Christiansen, K.5
  • 11
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • Dufour C, Dangles O (2005) Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy. BBA-General Subjects 1721: 164-173.
    • (2005) BBA-General Subjects 1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 12
    • 0033917295 scopus 로고    scopus 로고
    • Inhibition of human cytochrome P450 enzymes by constituents of St. John's Wort, an herbal preparation used in the treatment of depression
    • Obach RS (2000) Inhibition of human cytochrome P450 enzymes by constituents of St. John's Wort, an herbal preparation used in the treatment of depression. J Pharmacol Exp Ther 294: 88-95.
    • (2000) J Pharmacol Exp Ther , vol.294 , pp. 88-95
    • Obach, R.S.1
  • 13
    • 43049133223 scopus 로고    scopus 로고
    • Diniz A, Escuder-Gilabert L, Lopes NP, Rosa MaríaVillanueva- Camañas, Sagrado S, et al. (2008) Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis. Anal Bioanal Chem 391: 625-632.
    • Diniz A, Escuder-Gilabert L, Lopes NP, Rosa MaríaVillanueva- Camañas, Sagrado S, et al. (2008) Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis. Anal Bioanal Chem 391: 625-632.
  • 17
    • 0018580306 scopus 로고
    • Human Serum Albumin as a 'Silent Receptor' for Drugs and Endogenous Substances
    • Müller WE, Wollert U (1979) Human Serum Albumin as a 'Silent Receptor' for Drugs and Endogenous Substances. Pharmacology 19: 59-67.
    • (1979) Pharmacology , vol.19 , pp. 59-67
    • Müller, W.E.1    Wollert, U.2
  • 18
    • 33646377871 scopus 로고    scopus 로고
    • Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: A novel approach directly assigning binding site
    • Ahmad B, Parveen S, Khan RH (2006) Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site. Biomacromolecules 7: 1350-1356.
    • (2006) Biomacromolecules , vol.7 , pp. 1350-1356
    • Ahmad, B.1    Parveen, S.2    Khan, R.H.3
  • 19
    • 33846879203 scopus 로고    scopus 로고
    • Interactions of human serum albumin with retinoic acid, retinal and retinyl acetate
    • Karnaukhova E (2007) Interactions of human serum albumin with retinoic acid, retinal and retinyl acetate. Biochem Pharmacol 73: 901-910.
    • (2007) Biochem Pharmacol , vol.73 , pp. 901-910
    • Karnaukhova, E.1
  • 20
    • 45549084946 scopus 로고    scopus 로고
    • Temperature-dependent simultaneous ligand binding in human serum albumin
    • Sinha SS, Mitra RK, Pal SK (2008) Temperature-dependent simultaneous ligand binding in human serum albumin. J Phys Chem B 112: 4884-4891.
    • (2008) J Phys Chem B , vol.112 , pp. 4884-4891
    • Sinha, S.S.1    Mitra, R.K.2    Pal, S.K.3
  • 21
    • 38749139270 scopus 로고    scopus 로고
    • The interaction of silibinin with human serum albumin: A spectroscopic investigation
    • Maiti TK, Ghosh KS, Samanta A, Dasgupta S (2008) The interaction of silibinin with human serum albumin: A spectroscopic investigation. J Photochem Photobiol A 194: 297-307.
    • (2008) J Photochem Photobiol A , vol.194 , pp. 297-307
    • Maiti, T.K.1    Ghosh, K.S.2    Samanta, A.3    Dasgupta, S.4
  • 22
    • 40549103507 scopus 로고    scopus 로고
    • Binding of puerarin to human serum albumin: A spectroscopic analysis and molecular docking
    • He Y, Wang Y, Tang L, Liu H, Chen W, et al. (2008) Binding of puerarin to human serum albumin: a spectroscopic analysis and molecular docking. J Fluoresc 18: 433-442.
    • (2008) J Fluoresc , vol.18 , pp. 433-442
    • He, Y.1    Wang, Y.2    Tang, L.3    Liu, H.4    Chen, W.5
  • 23
    • 61949432567 scopus 로고    scopus 로고
    • Structural Analysis of Human Serum Albumin Complexes with Cationic Lipids
    • Charbonneau D, Beauregard M, Tajmir-Riahi HA (2009) Structural Analysis of Human Serum Albumin Complexes with Cationic Lipids. J Phys Chem B 113: 1777-1784.
    • (2009) J Phys Chem B , vol.113 , pp. 1777-1784
    • Charbonneau, D.1    Beauregard, M.2    Tajmir-Riahi, H.A.3
  • 24
    • 61449132323 scopus 로고    scopus 로고
    • Characterization of the mangiferin-human serum albumin complex by spectroscopic and molecular modeling approaches
    • Yue Y, Chen X, Qin J, Yao X (2009) Characterization of the mangiferin-human serum albumin complex by spectroscopic and molecular modeling approaches. J Pharm Biomed Anal 49: 753-759.
    • (2009) J Pharm Biomed Anal , vol.49 , pp. 753-759
    • Yue, Y.1    Chen, X.2    Qin, J.3    Yao, X.4
  • 25
    • 75449095230 scopus 로고    scopus 로고
    • Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, et al. (2010) Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 22: 77-87.
    • Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, et al. (2010) Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 22: 77-87.
  • 26
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter DC, Ho JX (1994) Structure of serum albumin. Adv Protein Chem 45: 153-203.
    • (1994) Adv Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 28
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He XM, Carter DC (1992) Atomic structure and chemistry of human serum albumin. Nature 358: 209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 29
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry S, Mandelkow H, Brick P, Franks N (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Mol Biol 5: 827-835.
    • (1998) Nat Struct Mol Biol , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 30
    • 0032720125 scopus 로고    scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • Curry S, Brick P, Frank NP (1999) Atomic structure and chemistry of human serum albumin. Biochim Biophys Acta 1441: 131-140.
    • (1999) Biochim Biophys Acta , vol.1441 , pp. 131-140
    • Curry, S.1    Brick, P.2    Frank, N.P.3
  • 31
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolution
    • Sugio S, Kashima A, Mochizuki S, Noda M, et al. (1999) Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng Des Sel 12: 439-446.
    • (1999) Protein Eng Des Sel , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4
  • 32
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya AA, Grüne T, Curry S (2000) Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J Mol Biol 303: 721-732.
    • (2000) J Mol Biol , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grüne, T.2    Curry, S.3
  • 33
    • 0035861982 scopus 로고    scopus 로고
    • Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids
    • Petitpas I, Grüne T, Bhattacharya AA, Curry S (2001) Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol 314: 955-960.
    • (2001) J Mol Biol , vol.314 , pp. 955-960
    • Petitpas, I.1    Grüne, T.2    Bhattacharya, A.A.3    Curry, S.4
  • 35
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin anatomy of drug site I
    • Petitpas I, Bhattacharya AA, Twine S, East M, Curry S (2001) Crystal structure analysis of warfarin binding to human serum albumin anatomy of drug site I. J Biol Chem 276: 22804-22809.
    • (2001) J Biol Chem , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 39
    • 40049109337 scopus 로고    scopus 로고
    • 3D-QSAR and docking studies of aminopyridine carboxamide inhibitors of c-Jun N-terminal kinase-1
    • Yi P, Qiu M (2008) 3D-QSAR and docking studies of aminopyridine carboxamide inhibitors of c-Jun N-terminal kinase-1. Eur J Med Chem 43: 604-613.
    • (2008) Eur J Med Chem , vol.43 , pp. 604-613
    • Yi, P.1    Qiu, M.2
  • 40
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC (1995) Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 245: 43-53.
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 41
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 43
    • 85016568461 scopus 로고    scopus 로고
    • Computational simulation of mitoxantrone binding with human serum albumin
    • Shahper NK, Asad UK (2008) Computational simulation of mitoxantrone binding with human serum albumin. J Proteomics Bioinform S1: S017-S020.
    • (2008) J Proteomics Bioinform S1
    • Shahper, N.K.1    Asad, U.K.2
  • 44
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer SS (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10: 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 45
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • Sulkowska A (2002) Interaction of drugs with bovine and human serum albumin. J Mol Struct 614: 227-232.
    • (2002) J Mol Struct , vol.614 , pp. 227-232
    • Sulkowska, A.1
  • 46
    • 42749083350 scopus 로고    scopus 로고
    • Mechanism of interaction between human serum albumin and N-alkyl phenothiazines studied using spectroscopic methods
    • Kandagal PB, Kalanur SS, Manjunatha DH, Seetharamappa J (2008) Mechanism of interaction between human serum albumin and N-alkyl phenothiazines studied using spectroscopic methods. J Pharm Biomed Anal 47: 260-267.
    • (2008) J Pharm Biomed Anal , vol.47 , pp. 260-267
    • Kandagal, P.B.1    Kalanur, S.S.2    Manjunatha, D.H.3    Seetharamappa, J.4
  • 48
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of ß-lactoglobulin with resveratrol and its biological implications
    • Liang L, Tajmir-Riahi HA, Subirade M (2007) Interaction of ß-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 9: 50-56.
    • (2007) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 49
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Kragh-Hansen U (1990) Structure and ligand binding properties of human serum albumin. Dan Med Bull 37: 57-84.
    • (1990) Dan Med Bull , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 50
    • 0036434544 scopus 로고    scopus 로고
    • The interaction of quercetin with human serum albumin: A fluorescence spectroscopic study
    • Sengupta B, Sengupta PK (2002) The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study. Biochem Biophys Res Commun 299: 400-403.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 400-403
    • Sengupta, B.1    Sengupta, P.K.2
  • 51
    • 44649095723 scopus 로고    scopus 로고
    • Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin
    • Jiang YL (2008) Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin. Bioorgan Med Chem 16: 6406-6414.
    • (2008) Bioorgan Med Chem , vol.16 , pp. 6406-6414
    • Jiang, Y.L.1
  • 52
    • 9144221136 scopus 로고    scopus 로고
    • Binding of genistein to human serum albumin demonstrated using tryptophan fluorescence quenching
    • Bian Q, Liu J, Tian J, Hu Z (2004) Binding of genistein to human serum albumin demonstrated using tryptophan fluorescence quenching. Int J Biol Macromol 34: 275-279.
    • (2004) Int J Biol Macromol , vol.34 , pp. 275-279
    • Bian, Q.1    Liu, J.2    Tian, J.3    Hu, Z.4
  • 53
    • 0037300833 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods
    • Zsila F, Bikbdi Z, Simonyi M (2003) Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods. Biochem Pharmacol 65: 447-456.
    • (2003) Biochem Pharmacol , vol.65 , pp. 447-456
    • Zsila, F.1    Bikbdi, Z.2    Simonyi, M.3
  • 56
    • 0031896612 scopus 로고    scopus 로고
    • Species differences of serum albumins: II. Chemical and thermal stability
    • Kosa T, Maruyama T, Otagiri M (1998) Species differences of serum albumins: II. Chemical and thermal stability. Pharmaceut Res 15: 449-454.
    • (1998) Pharmaceut Res , vol.15 , pp. 449-454
    • Kosa, T.1    Maruyama, T.2    Otagiri, M.3
  • 57
    • 59949097010 scopus 로고    scopus 로고
    • Molecular interactions of isoxazolcurcumin with human serum albumin: Spectroscopic and molecular modeling studies
    • BK S, Ghosh GKS, Dasgupta DS (2009) Molecular interactions of isoxazolcurcumin with human serum albumin: spectroscopic and molecular modeling studies. Biopolymers 91: 108-119.
    • (2009) Biopolymers , vol.91 , pp. 108-119
    • BK, S.1    Ghosh, G.K.S.2    Dasgupta, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.