메뉴 건너뛰기




Volumn 398, Issue 3, 2010, Pages 444-449

Flavonoid binding to human serum albumin

Author keywords

Allostery; Daidzein; Daidzein metabolites; Flavonoid binding; Genistein; Human serum albumin; Naringenin; Oleate; Quercetin; Thermodynamics

Indexed keywords

4' DAIDZEINSULFATE; 4',7 DAIDZEINDISULFATE; 6,3' DIHYDROXYDAIDZEIN; 7 DAIDZEINSULFATE; 8 HYDROXYDAIDZEIN; 8,3' DIHYDROXYDAIDZEIN; DAIDZEIN; FLAVONOID; GENISTEIN; HUMAN SERUM ALBUMIN; NARINGENIN; QUERCETIN; UNCLASSIFIED DRUG;

EID: 77955276013     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.096     Document Type: Article
Times cited : (110)

References (47)
  • 1
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., Wade D.N. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 1975, 11:824-832.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 3
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • Kragh-Hansen U., Chuang V.T., Otagiri M. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol. Pharm. Bull. 2002, 25:695-704.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 695-704
    • Kragh-Hansen, U.1    Chuang, V.T.2    Otagiri, M.3
  • 7
    • 3042673067 scopus 로고    scopus 로고
    • Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
    • Zunszain P.A., Ghuman J., Komatsu T., Tsuchida E., Curry S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Struct. Biol. 2003, 3:6.
    • (2003) BMC Struct. Biol. , vol.3 , pp. 6
    • Zunszain, P.A.1    Ghuman, J.2    Komatsu, T.3    Tsuchida, E.4    Curry, S.5
  • 8
    • 77449098529 scopus 로고    scopus 로고
    • Serum heme-albumin: an allosteric protein
    • Ascenzi P., Fasano M. Serum heme-albumin: an allosteric protein. IUBMB Life 2009, 61:1118-1122.
    • (2009) IUBMB Life , vol.61 , pp. 1118-1122
    • Ascenzi, P.1    Fasano, M.2
  • 10
    • 77951977240 scopus 로고    scopus 로고
    • Allostery in a monomeric protein: the case of human serum heme-albumin
    • Ascenzi P., Fasano M. Allostery in a monomeric protein: the case of human serum heme-albumin. Biophys. Chem. 2010, 148:16-22.
    • (2010) Biophys. Chem. , vol.148 , pp. 16-22
    • Ascenzi, P.1    Fasano, M.2
  • 11
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry S., Mandelkov H., Brick P., Franks N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 1998, 5:827-835.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkov, H.2    Brick, P.3    Franks, N.4
  • 12
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures
    • Bhattacharya A.A., Curry S., Franks N.P. Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J. Biol. Chem. 2000, 275:38731-38738.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 13
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya A.A., Grüne T., Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 2000, 303:721-732.
    • (2000) J. Mol. Biol. , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grüne, T.2    Curry, S.3
  • 14
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I
    • Petitpas I., Bhattacharya A.A., Twine S., East M., Curry S. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J. Biol. Chem. 2001, 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
  • 15
    • 0036804804 scopus 로고    scopus 로고
    • How do fatty acids cause allosteric binding of drugs to human serum albumin?
    • Chuang V.T.G., Otagiri M. How do fatty acids cause allosteric binding of drugs to human serum albumin?. Pharm. Res. 2002, 19:1458-1464.
    • (2002) Pharm. Res. , vol.19 , pp. 1458-1464
    • Chuang, V.T.G.1    Otagiri, M.2
  • 16
    • 1542345719 scopus 로고    scopus 로고
    • Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us
    • Hamilton J.A. Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us. Prog. Lipid. Res. 2004, 43:177-199.
    • (2004) Prog. Lipid. Res. , vol.43 , pp. 177-199
    • Hamilton, J.A.1
  • 17
    • 70350455500 scopus 로고    scopus 로고
    • Lessons from the crystallographic analysis of small molecule binding to human serum albumin
    • Curry S. Lessons from the crystallographic analysis of small molecule binding to human serum albumin. Drug Metab. Pharmacokinet. 2009, 24:342-357.
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 342-357
    • Curry, S.1
  • 18
    • 42549108676 scopus 로고    scopus 로고
    • Nutritional flavonoids impact on nuclear and extranuclear estrogen receptor activities
    • Galluzzo P., Marino M. Nutritional flavonoids impact on nuclear and extranuclear estrogen receptor activities. Genes Nutr. 2006, 1:161-176.
    • (2006) Genes Nutr. , vol.1 , pp. 161-176
    • Galluzzo, P.1    Marino, M.2
  • 19
    • 77951107225 scopus 로고    scopus 로고
    • Mechanisms at the root of flavonoid action in cancer: a step toward solving the Rubik's cube
    • Nova Science Publishers, New York, R.B. Keller (Ed.)
    • Marino M., Bulzomi P. Mechanisms at the root of flavonoid action in cancer: a step toward solving the Rubik's cube. Flavonoids: Biosynthesis Biological Effects and Dietary Sources 2009, 231-248. Nova Science Publishers, New York. R.B. Keller (Ed.).
    • (2009) Flavonoids: Biosynthesis Biological Effects and Dietary Sources , pp. 231-248
    • Marino, M.1    Bulzomi, P.2
  • 20
    • 53549087775 scopus 로고    scopus 로고
    • Regulation of cellular signals from nutritional molecules: a specific role for phytochemicals, beyond antioxidant activity
    • Virgili F., Marino M. Regulation of cellular signals from nutritional molecules: a specific role for phytochemicals, beyond antioxidant activity. Free Radic. Biol. Med. 2008, 45:1205-1216.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1205-1216
    • Virgili, F.1    Marino, M.2
  • 21
    • 69949105336 scopus 로고    scopus 로고
    • From functional food to medicinal product: systematic approach in analysis of polyphenolics from propolis and wine
    • Medić-Sarić M., Rastija V., Bojić M., Males Z. From functional food to medicinal product: systematic approach in analysis of polyphenolics from propolis and wine. Nutr. J. 2009, 8:33.
    • (2009) Nutr. J. , vol.8 , pp. 33
    • Medić-Sarić, M.1    Rastija, V.2    Bojić, M.3    Males, Z.4
  • 24
    • 29144461887 scopus 로고    scopus 로고
    • Allosteric modulation of anti-HIV drug and ferric heme binding to human serum albumin
    • Bocedi A., Notari S., Menegatti E., Fanali G., Fasano M., Ascenzi P. Allosteric modulation of anti-HIV drug and ferric heme binding to human serum albumin. FEBS J. 2005, 272:6287-6296.
    • (2005) FEBS J. , vol.272 , pp. 6287-6296
    • Bocedi, A.1    Notari, S.2    Menegatti, E.3    Fanali, G.4    Fasano, M.5    Ascenzi, P.6
  • 27
    • 0014409249 scopus 로고
    • The binding of carbon monoxide by human hemoglobin: proof of validity of the spectrophotometric method and direct determination of the equilibrium
    • Anderson S.R., Antonini E. The binding of carbon monoxide by human hemoglobin: proof of validity of the spectrophotometric method and direct determination of the equilibrium. J. Biol. Chem. 1968, 243:2918-2920.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2918-2920
    • Anderson, S.R.1    Antonini, E.2
  • 28
    • 0034684222 scopus 로고    scopus 로고
    • 2S solubility via the reaction with ferric hemoglobin I from the bivalve mollusc Lucina pectinata
    • 2S solubility via the reaction with ferric hemoglobin I from the bivalve mollusc Lucina pectinata. Biochim. Biophys. Acta 2000, 1523:206-208.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 206-208
    • Boffi, A.1    Rizzi, M.2    Monacelli, F.3    Ascenzi, P.4
  • 29
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell D.S., Olson A.J. Automated docking of substrates to proteins by simulated annealing. Proteins 1990, 8:195-202.
    • (1990) Proteins , vol.8 , pp. 195-202
    • Goodsell, D.S.1    Olson, A.J.2
  • 30
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: applications of autodock
    • Goodsell D.S., Morris G.M., Olson A.J. Automated docking of flexible ligands: applications of autodock. J. Mol. Recogn. 1998, 9:1-5.
    • (1998) J. Mol. Recogn. , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 32
    • 0035861982 scopus 로고    scopus 로고
    • Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids
    • Petitpas I., Grüne T., Bhattacharya A.A., Curry S. Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J. Mol. Biol. 2001, 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
  • 33
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuettelkopf A.W., Van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:1355-1363.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schuettelkopf, A.W.1    Van Aalten, D.M.2
  • 34
    • 0020081536 scopus 로고
    • Fluorimetric analysis of the binding of warfarin to human serum albumin: equilibrium and kinetic study
    • Maes V., Engelborghs Y., Hoebeke J., Maras Y., Vercruysse A. Fluorimetric analysis of the binding of warfarin to human serum albumin: equilibrium and kinetic study. Mol. Pharmacol. 1982, 21:100-107.
    • (1982) Mol. Pharmacol. , vol.21 , pp. 100-107
    • Maes, V.1    Engelborghs, Y.2    Hoebeke, J.3    Maras, Y.4    Vercruysse, A.5
  • 36
    • 2642586736 scopus 로고    scopus 로고
    • Competition of drugs to serum albumin in combination therapy
    • Sułkowska A., Bojko B., Równicka J., Sułkowski W. Competition of drugs to serum albumin in combination therapy. Biopolymers 2004, 74:256-262.
    • (2004) Biopolymers , vol.74 , pp. 256-262
    • Sułkowska, A.1    Bojko, B.2    Równicka, J.3    Sułkowski, W.4
  • 38
    • 38349120997 scopus 로고    scopus 로고
    • Fluorescence quenching of serum albumin by rifampycin antibiotics and their analytical application
    • Yang J.D., Deng S.X., Liu Z.F., Kong L., Liu S.P. Fluorescence quenching of serum albumin by rifampycin antibiotics and their analytical application. Luminescence 2007, 22:559-566.
    • (2007) Luminescence , vol.22 , pp. 559-566
    • Yang, J.D.1    Deng, S.X.2    Liu, Z.F.3    Kong, L.4    Liu, S.P.5
  • 39
    • 77953607291 scopus 로고    scopus 로고
    • Binding of anti-Parkinson's disease drugs to human serum albumin is allosterically modulated
    • Fanali G., Rampoldi V., Di Masi A., Bolli A., Lopiano L., Ascenzi P., Fasano M. Binding of anti-Parkinson's disease drugs to human serum albumin is allosterically modulated. IUBMB Life 2010, 62:371-376.
    • (2010) IUBMB Life , vol.62 , pp. 371-376
    • Fanali, G.1    Rampoldi, V.2    Di Masi, A.3    Bolli, A.4    Lopiano, L.5    Ascenzi, P.6    Fasano, M.7
  • 40
    • 77951533737 scopus 로고    scopus 로고
    • Interactions between quercetin and warfarin for albumin binding: a new eye on food/drug interference
    • Di Bari L., Ripoli S., Pradhan S., Salvadori P. Interactions between quercetin and warfarin for albumin binding: a new eye on food/drug interference. Chirality 2010, 22:593-596.
    • (2010) Chirality , vol.22 , pp. 593-596
    • Di Bari, L.1    Ripoli, S.2    Pradhan, S.3    Salvadori, P.4
  • 41
    • 33746253976 scopus 로고    scopus 로고
    • Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis
    • Simard J.R., Zunszain P.A., Hamilton J.A., Curry S. Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis. J. Mol. Biol. 2006, 361:336-351.
    • (2006) J. Mol. Biol. , vol.361 , pp. 336-351
    • Simard, J.R.1    Zunszain, P.A.2    Hamilton, J.A.3    Curry, S.4
  • 42
    • 42549141260 scopus 로고    scopus 로고
    • The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptor α-palmitoylation
    • Galluzzo P., Ascenzi P., Bulzomi P., Marino M. The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptor α-palmitoylation. Endocrinology 2008, 149:2567-2575.
    • (2008) Endocrinology , vol.149 , pp. 2567-2575
    • Galluzzo, P.1    Ascenzi, P.2    Bulzomi, P.3    Marino, M.4
  • 43
    • 68149124472 scopus 로고    scopus 로고
    • Dietary phenolics: chemistry, bioavailability and effects on health
    • Crozier A., Jaganath I.B., Clifford M.N. Dietary phenolics: chemistry, bioavailability and effects on health. Nat. Prod. Rep. 2009, 26:1001-1043.
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1001-1043
    • Crozier, A.1    Jaganath, I.B.2    Clifford, M.N.3
  • 44
    • 31544448040 scopus 로고    scopus 로고
    • Daidzein-sulfate metabolites affect transcriptional and antiproliferative activities of estrogen receptor-β in cultured human cancer cells
    • Totta P., Acconcia F., Virgili F., Cassidy A., Weinberg P.D., Rimbach G., Marino M. Daidzein-sulfate metabolites affect transcriptional and antiproliferative activities of estrogen receptor-β in cultured human cancer cells. J. Nutr. 2005, 135:2687-2693.
    • (2005) J. Nutr. , vol.135 , pp. 2687-2693
    • Totta, P.1    Acconcia, F.2    Virgili, F.3    Cassidy, A.4    Weinberg, P.D.5    Rimbach, G.6    Marino, M.7
  • 45
    • 46049112534 scopus 로고    scopus 로고
    • Vegetable flavonoids and cardiovascular disease
    • Terao J., Kawai Y., Murota K. Vegetable flavonoids and cardiovascular disease. Asia Pac. J. Clin. Nutr. 2008, 17(Suppl 1):291-293.
    • (2008) Asia Pac. J. Clin. Nutr. , vol.17 , Issue.SUPPL. 1 , pp. 291-293
    • Terao, J.1    Kawai, Y.2    Murota, K.3
  • 46
    • 77951226251 scopus 로고    scopus 로고
    • Beyond obesity: the diagnosis and pathophysiology of metabolic syndrome
    • Gade W., Schmit J., Collins M., Gade J. Beyond obesity: the diagnosis and pathophysiology of metabolic syndrome. Clin. Lab. Sci. 2010, 23:51-61.
    • (2010) Clin. Lab. Sci. , vol.23 , pp. 51-61
    • Gade, W.1    Schmit, J.2    Collins, M.3    Gade, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.