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Volumn 56, Issue 17, 2008, Pages 7721-7729

Binding of phenolic compounds and their derivatives to bovine and reindeer β-lactoglobulin

Author keywords

Lactoglobulins; Binding; Flavonols; Fluorescence; Phenolic compounds

Indexed keywords

CATECHIN; COUMARIN DERIVATIVE; FLAVONOID; LACTOGLOBULIN; PHENOL DERIVATIVE;

EID: 52649138940     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf801120a     Document Type: Article
Times cited : (87)

References (57)
  • 1
    • 0032400815 scopus 로고    scopus 로고
    • Flavonoids: Dietary occurrence and biochemical activity
    • Peterson, J.; Dwyer, J. Flavonoids: dietary occurrence and biochemical activity. Nutr. Res. (N.Y.) 1998, 18, 1995-2018.
    • (1998) Nutr. Res. (N.Y.) , vol.18 , pp. 1995-2018
    • Peterson, J.1    Dwyer, J.2
  • 2
    • 85026737771 scopus 로고    scopus 로고
    • Flavonoids in foods
    • Andersen, Q. M, Markham, K. R, Eds, CRC Press, Taylor & Francis Group: Boca Raton, FL
    • Kyle, J. A. M.; Duthie, G. G. Flavonoids in foods. In Flavonoids: Chemistry, Biochemistry and Applications; Andersen, Q. M., Markham, K. R., Eds.; CRC Press, Taylor & Francis Group: Boca Raton, FL, 2006; Vol. 4, pp 219-262.
    • (2006) Flavonoids: Chemistry, Biochemistry and Applications , vol.4 , pp. 219-262
    • Kyle, J.A.M.1    Duthie, G.G.2
  • 3
    • 0036928722 scopus 로고    scopus 로고
    • Measuring flavonoid intake: Need for advanced tools
    • Dwyer, J. T.; Peterson, J. J. Measuring flavonoid intake: need for advanced tools. Public Health Nutr. 2002, 5, 925-930.
    • (2002) Public Health Nutr , vol.5 , pp. 925-930
    • Dwyer, J.T.1    Peterson, J.J.2
  • 5
    • 0030775534 scopus 로고    scopus 로고
    • Absorption, metabolism and health effects of dietary flavonoids in man
    • Hollman, P. C.; Katan, M. B. Absorption, metabolism and health effects of dietary flavonoids in man. Biomed. Pharmacother. 1997, 51, 305-310.
    • (1997) Biomed. Pharmacother , vol.51 , pp. 305-310
    • Hollman, P.C.1    Katan, M.B.2
  • 6
    • 0037048763 scopus 로고    scopus 로고
    • Antiproliferative activities of citrus flavonoids against six human cancer cell lines
    • Manthey, J. A.; Guthrie, N. Antiproliferative activities of citrus flavonoids against six human cancer cell lines. J. Agric. Food Chem. 2002, 50, 5837-5843.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 5837-5843
    • Manthey, J.A.1    Guthrie, N.2
  • 7
    • 0036400016 scopus 로고    scopus 로고
    • Dietary flavonoids: Bioavailability, metabolic effects, and safety
    • Ross, J. A.; Kasum, C. M. Dietary flavonoids: bioavailability, metabolic effects, and safety. Annu. Rev. Nutr. 2002, 22, 19-34.
    • (2002) Annu. Rev. Nutr , vol.22 , pp. 19-34
    • Ross, J.A.1    Kasum, C.M.2
  • 10
    • 11844269306 scopus 로고    scopus 로고
    • Flavonoid glucosides are hydrolyzed and thus activated in the oral cavity in humans
    • Walle, T.; Browning, A. M.; Steed, L. L.; Reed, S. G.; Walle, U. K. Flavonoid glucosides are hydrolyzed and thus activated in the oral cavity in humans. J. Nutr. 2005, 135, 48-52.
    • (2005) J. Nutr , vol.135 , pp. 48-52
    • Walle, T.1    Browning, A.M.2    Steed, L.L.3    Reed, S.G.4    Walle, U.K.5
  • 11
    • 0343061059 scopus 로고    scopus 로고
    • Effect of the stability of plant phenolic compounds
    • Friedman, M.; Jürgens, H. S. Effect of the stability of plant phenolic compounds. J. Agric. Food Chem. 2000, 48, 2101-2110.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 2101-2110
    • Friedman, M.1    Jürgens, H.S.2
  • 12
    • 34249861380 scopus 로고    scopus 로고
    • Thermal degradation of onion quercetin glucosides under roasting conditions
    • Rohn, S.; Buchner, N.; Driemel, G.; Rauser, M.; Kroh, L. W. Thermal degradation of onion quercetin glucosides under roasting conditions. J. Agric. Food Chem. 2007, 55, 1568-1573.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 1568-1573
    • Rohn, S.1    Buchner, N.2    Driemel, G.3    Rauser, M.4    Kroh, L.W.5
  • 13
    • 33750298551 scopus 로고    scopus 로고
    • Effect of thermal processing on the flavonols rutin and quercetin
    • Buchner, N.; Krumbein, A.; Rohn, S.; Kroh, L. W. Effect of thermal processing on the flavonols rutin and quercetin. Rapid Commun. Mass Spectrom. 2006, 20, 3229-3235.
    • (2006) Rapid Commun. Mass Spectrom , vol.20 , pp. 3229-3235
    • Buchner, N.1    Krumbein, A.2    Rohn, S.3    Kroh, L.W.4
  • 14
    • 0004187143 scopus 로고    scopus 로고
    • 3rd; ed, Fox, P. F, McSweeney, P. L. H, Eds, Kluwer Academic/Plenum Publisher: New York, 322 pp
    • Sawyer, L. β-Lactoglobulin. In Advanced Dairy Chemistry - 1 Proteins, 3rd; ed.; Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publisher: New York, 2003; Vol. 7, 322 pp.
    • (2003) Advanced Dairy Chemistry - 1 Proteins , vol.7
    • Sawyer1    β-Lactoglobulin, L.2
  • 15
    • 0029302371 scopus 로고
    • Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review
    • Perez, M. D.; Calvo, M. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J. Dairy Sci. 1995, 78, 978-988.
    • (1995) J. Dairy Sci , vol.78 , pp. 978-988
    • Perez, M.D.1    Calvo, M.2
  • 16
    • 0031160714 scopus 로고    scopus 로고
    • Binding of vitamin D and cholesterol to β-lactoglobulin
    • Wang, Q.; Allen, J. C.; Swaisgood, H. E. Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci. 1997, 80, 1054-1059.
    • (1997) J. Dairy Sci , vol.80 , pp. 1054-1059
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 17
    • 0031160713 scopus 로고    scopus 로고
    • Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption
    • Wang, Q.; Allen, J. C.; Swaisgood, H. E. Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption. J. Dairy Sci. 1997, 80, 1047-1053.
    • (1997) J. Dairy Sci , vol.80 , pp. 1047-1053
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 18
    • 0036890385 scopus 로고    scopus 로고
    • Retinoic acid binding properties of the lipocalin member β-lactoglobulin studied by circular dichroism, electronic absorption spectroscopy and molecular modeling methods
    • Zsila, F.; Bikadi, Z.; Simonyi, M. Retinoic acid binding properties of the lipocalin member β-lactoglobulin studied by circular dichroism, electronic absorption spectroscopy and molecular modeling methods. Biochem. Pharmacol. 2002, 64, 1651-1660.
    • (2002) Biochem. Pharmacol , vol.64 , pp. 1651-1660
    • Zsila, F.1    Bikadi, Z.2    Simonyi, M.3
  • 25
    • 0032483094 scopus 로고    scopus 로고
    • Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer
    • Lange, D. C.; Kothari, R.; Patel, R. C.; Patel, S. C. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys. Chem. 1998, 74, 45-51.
    • (1998) Biophys. Chem , vol.74 , pp. 45-51
    • Lange, D.C.1    Kothari, R.2    Patel, R.C.3    Patel, S.C.4
  • 26
    • 30744474722 scopus 로고    scopus 로고
    • Characterization of local polarity and hydrophobic binding sites of β-lactoglobulin by using N-terminal specific fluorescence labeling
    • Dong, S. Y.; Zhao, Z. W.; Ma, H. M. Characterization of local polarity and hydrophobic binding sites of β-lactoglobulin by using N-terminal specific fluorescence labeling. J. Proteome Res. 2006, 5, 26-31.
    • (2006) J. Proteome Res , vol.5 , pp. 26-31
    • Dong, S.Y.1    Zhao, Z.W.2    Ma, H.M.3
  • 29
    • 0036014415 scopus 로고    scopus 로고
    • Isolation and characterization of β-lactoglobulin from reindeer milk
    • Rytkönen, J.; Alatossava, T.; Nieminen, M.; Valkonen, K. Isolation and characterization of β-lactoglobulin from reindeer milk. Milchwissenschaft 2002, 57, 259-261.
    • (2002) Milchwissenschaft , vol.57 , pp. 259-261
    • Rytkönen, J.1    Alatossava, T.2    Nieminen, M.3    Valkonen, K.4
  • 32
    • 0036073857 scopus 로고    scopus 로고
    • Interaction of plant polyphenols with salivary proteins
    • Bennick, A. Interaction of plant polyphenols with salivary proteins. Crit. Rev. Oral Biol. Med. 2002, 13, 184-196.
    • (2002) Crit. Rev. Oral Biol. Med , vol.13 , pp. 184-196
    • Bennick, A.1
  • 33
    • 0035290424 scopus 로고    scopus 로고
    • Mild isolation procedure discloses new protein structural properties of β-lactoglobulin
    • de Jongh, H. H.; Groneveld, T.; de Groot, J. Mild isolation procedure discloses new protein structural properties of β-lactoglobulin. J. Dairy Sci. 2001, 84, 562-571.
    • (2001) J. Dairy Sci , vol.84 , pp. 562-571
    • de Jongh, H.H.1    Groneveld, T.2    de Groot, J.3
  • 36
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren, T. A.; Murphy, R. B.; Friesner, R. A.; Beard, H. S.; Frye, L. L.; Pollard, W. T.; Banks, J. L. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J. Med. Chem. 2004, 47, 1750-1759.
    • (2004) J. Med. Chem , vol.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 37
    • 0000490166 scopus 로고
    • From atoms and bonds to 3-dimensional atomic coordinates: Automatic model builders
    • Sadowski, J.; Gasteiger, J. From atoms and bonds to 3-dimensional atomic coordinates: automatic model builders. Chem. Rev. 1993, 93, 2567-2581.
    • (1993) Chem. Rev , vol.93 , pp. 2567-2581
    • Sadowski, J.1    Gasteiger, J.2
  • 38
    • 0036037132 scopus 로고    scopus 로고
    • The ligand-binding site of bovine β-lactoglobulin: Evidence for a function?
    • Kontopidis, G.; Holt, C.; Sawyer, L. The ligand-binding site of bovine β-lactoglobulin: evidence for a function? J. Mol. Biol. 2002, 318, 1043-1055.
    • (2002) J. Mol. Biol , vol.318 , pp. 1043-1055
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 40
    • 0017075905 scopus 로고
    • Binding affinities of retinol and related compounds to retinol binding proteins
    • Cogan, U.; Kopelman, M.; Mokady, S.; Shinitzky, M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 1976, 65, 71-78.
    • (1976) Eur. J. Biochem , vol.65 , pp. 71-78
    • Cogan, U.1    Kopelman, M.2    Mokady, S.3    Shinitzky, M.4
  • 41
    • 0033048388 scopus 로고    scopus 로고
    • Daidzein and genistein but not their glucosides are absorbed from the rat stomach
    • Piskula, M. K.; Yamakoshi, J.; Iwai, Y. Daidzein and genistein but not their glucosides are absorbed from the rat stomach. FEBS Lett. 1999, 447, 287-291.
    • (1999) FEBS Lett , vol.447 , pp. 287-291
    • Piskula, M.K.1    Yamakoshi, J.2    Iwai, Y.3
  • 42
    • 0032524982 scopus 로고    scopus 로고
    • Transport of quercetin and ist glucosides across human intestinal epithelial caco-2 cells
    • Walgren, R. A.; Walle, U. K.; Walle, T. Transport of quercetin and ist glucosides across human intestinal epithelial caco-2 cells. Biochem. Pharmacol. 1998, 55, 1721-1727.
    • (1998) Biochem. Pharmacol , vol.55 , pp. 1721-1727
    • Walgren, R.A.1    Walle, U.K.2    Walle, T.3
  • 44
    • 33746483941 scopus 로고    scopus 로고
    • Interactions between bovine β-lactoglobulin A and various bioactive peptides as studied by front-face fluorescence spectroscopy
    • Roufik, S.; Gauthier, S. F.; Dufour, E.; Turgeon, S. L. Interactions between bovine β-lactoglobulin A and various bioactive peptides as studied by front-face fluorescence spectroscopy. J. Agric. Food Chem. 2006, 54, 4962-4969.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 4962-4969
    • Roufik, S.1    Gauthier, S.F.2    Dufour, E.3    Turgeon, S.L.4
  • 45
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence
    • Manderson, G. A.; Hardman, M. J.; Creamer, L. K. Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 1999, 47, 3617-3627.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 46
    • 34548051331 scopus 로고    scopus 로고
    • Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary α-amylase (HSA) by fluorescence quenching
    • Soares, S.; Mateus, N.; Freitas, V. Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary α-amylase (HSA) by fluorescence quenching. J. Agric. Food Chem. 2007, 55, 6726-6735.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 6726-6735
    • Soares, S.1    Mateus, N.2    Freitas, V.3
  • 47
    • 0042387727 scopus 로고    scopus 로고
    • Influence of a sugar moiety (rhamnosylglucoside) at 3-O position on the reactivity of quercetin with whey proteins
    • Rawel, H. M.; Rohn, S.; Kroll, J. Influence of a sugar moiety (rhamnosylglucoside) at 3-O position on the reactivity of quercetin with whey proteins. Int. J. Biol. Macromol. 2003, 32, 109-120.
    • (2003) Int. J. Biol. Macromol , vol.32 , pp. 109-120
    • Rawel, H.M.1    Rohn, S.2    Kroll, J.3
  • 48
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern, S. L.; Caselli, E.; Grigorieff, N.; Shoichet, B. K. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J. Med. Chem. 2002, 45, 1712-1722.
    • (2002) J. Med. Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 49
    • 0141755209 scopus 로고    scopus 로고
    • EF loop conformational change triggers ligand binding in β-lactoglobulins
    • Ragona, L.; Fogolari, F.; Catalano, M.; Ugolini, R.; Zetta, L.; Molinari, H. EF loop conformational change triggers ligand binding in β-lactoglobulins. J. Biol. Chem. 2003, 278, 38840-38846.
    • (2003) J. Biol. Chem , vol.278 , pp. 38840-38846
    • Ragona, L.1    Fogolari, F.2    Catalano, M.3    Ugolini, R.4    Zetta, L.5    Molinari, H.6
  • 50
    • 0001497241 scopus 로고
    • The reversible transformation of β-lactoglobulin at pH 7.5
    • Tanford, B. C.; Bunville, L. G; Nozaki, Y. The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 1959, 81, 4032-4036.
    • (1959) J. Am. Chem. Soc , vol.81 , pp. 4032-4036
    • Tanford, B.C.1    Bunville, L.G.2    Nozaki, Y.3
  • 52
    • 30544433324 scopus 로고    scopus 로고
    • Binding of the pepper alkaloid pipeline to bovine β-lactoglobulin: Circular dichroism spectroscopy and molecular modeling study
    • Zsila, F.; Hazai, E.; Sawyer, L. Binding of the pepper alkaloid pipeline to bovine β-lactoglobulin: circular dichroism spectroscopy and molecular modeling study. J. Agric. Food Chem. 2005, 53, 10179-10185.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 10179-10185
    • Zsila, F.1    Hazai, E.2    Sawyer, L.3
  • 53
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with resveratrol and its biological implications
    • Liang, L.; Tajmir-Riahi, H. A.; Subirade, M. Interaction of β-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 2008, 9, 50-56.
    • (2008) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 54
    • 0036198482 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins
    • Andrade, S. M.; Costa, S. M. Spectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins. Biophys. J. 2002, 82, 1607-1619.
    • (2002) Biophys. J , vol.82 , pp. 1607-1619
    • Andrade, S.M.1    Costa, S.M.2
  • 55
    • 33750469308 scopus 로고    scopus 로고
    • Heat and pH effects on the conjugated forms of genistin and daidzin isoflavones
    • Mathias, K.; Ismail, B.; Corvalan, C. M.; Hayes, K. D. Heat and pH effects on the conjugated forms of genistin and daidzin isoflavones. J. Agric. Food Chem. 2006, 54, 7495-7502.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 7495-7502
    • Mathias, K.1    Ismail, B.2    Corvalan, C.M.3    Hayes, K.D.4
  • 56
    • 34247188964 scopus 로고    scopus 로고
    • Effect of storage conditions on the biological activity of phenolic compounds of blueberry extract packed in glass bottles
    • Srivastava, A.; Akoh, C. C.; Yi, W.; Fischer, J.; Krewer, G. Effect of storage conditions on the biological activity of phenolic compounds of blueberry extract packed in glass bottles. J. Agric. Food Chem. 2007, 55, 2705-2713.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 2705-2713
    • Srivastava, A.1    Akoh, C.C.2    Yi, W.3    Fischer, J.4    Krewer, G.5
  • 57
    • 84903421858 scopus 로고    scopus 로고
    • Introduction: Classifying functional dairy products
    • Mattila-Sandholm, T, Saarela, M, Eds, Woodhead Publishing: Cambridge, U.K
    • Saxelin, M.; Korpela, R.; Mäyrä-Mäkinen, A. Introduction: classifying functional dairy products. In Functional Dairy Products; Mattila-Sandholm, T., Saarela, M., Eds.; Woodhead Publishing: Cambridge, U.K., 2003; Vol. 1, p 4.
    • (2003) Functional Dairy Products , vol.1 , pp. 4
    • Saxelin, M.1    Korpela, R.2    Mäyrä-Mäkinen, A.3


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