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Volumn 117, Issue 5, 2013, Pages 1287-1295

Binding sites of resveratrol, genistein, and curcumin with milk α- And β-caseins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CONFORMATIONS; FLAVONOIDS; MOLECULAR MODELING; PHENOLS; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 84873453386     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp3114557     Document Type: Article
Times cited : (157)

References (49)
  • 1
    • 79952381343 scopus 로고    scopus 로고
    • On the Structural Models of Bovine Casein Micelles-Review and Possible Improvements
    • Dalgleish, D. G. On the Structural Models of Bovine Casein Micelles-Review and Possible Improvements Soft Matter 2011, 7, 2265-2272
    • (2011) Soft Matter , vol.7 , pp. 2265-2272
    • Dalgleish, D.G.1
  • 2
    • 0036128797 scopus 로고    scopus 로고
    • Natively Unfolded Proteins: Appoint Where Biology Waits for Physics
    • Uversky, V. N. Natively Unfolded Proteins: Appoint Where Biology Waits for Physics Protein Sci. 2002, 11, 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 4
    • 0027586726 scopus 로고
    • Three-Dimensional Molecular Modeling of Bovine Caseins: A Refined, Energy-Minimized Beta-Casein Structure
    • Kumosinski, T. F.; Brown, E. M.; Farell, H. M., Jr. Three-Dimensional Molecular Modeling of Bovine Caseins: A Refined, Energy-Minimized Beta-Casein Structure J. Dairy Sci. 1993, 76, 931-945
    • (1993) J. Dairy Sci. , vol.76 , pp. 931-945
    • Kumosinski, T.F.1    Brown, E.M.2    Farell Jr., H.M.3
  • 6
    • 33845904590 scopus 로고    scopus 로고
    • Casein Micelle Structure: A Concise Review
    • Phadungath, C. Casein Micelle Structure: A Concise Review J. Sci. Technol. 2005, 27, 201-212
    • (2005) J. Sci. Technol. , vol.27 , pp. 201-212
    • Phadungath, C.1
  • 7
    • 0002772383 scopus 로고
    • Chemistry of Caseins
    • In, Vol. Proteins; Fox, P. F. Elsevier Science Publisher, Ltd. Essex
    • Swaisgood, H. E. Chemistry of Caseins. In Advanced Dairy Chemistry, Vol. 1: Proteins; Fox, P. F., Ed.; Elsevier Science Publisher, Ltd.: Essex, 1992; pp 63-110.
    • (1992) Advanced Dairy Chemistry , vol.1 , pp. 63-110
    • Swaisgood, H.E.1
  • 8
    • 0037699038 scopus 로고    scopus 로고
    • Effect of Extraction Temperature on Cream and Extractibility of Black Tea [ Camellia sinensis (L.) O. Kuntze]
    • Liang, Y.; Xu, Y. Effect of Extraction Temperature on Cream and Extractibility of Black Tea [ Camellia sinensis (L.) O. Kuntze] Int. J. Food Sci. Technol. 2003, 38, 37-45
    • (2003) Int. J. Food Sci. Technol. , vol.38 , pp. 37-45
    • Liang, Y.1    Xu, Y.2
  • 10
    • 77957346768 scopus 로고    scopus 로고
    • Beta-Casein Nanoparticles as an Oral Delivery System for Chemotherapeutic Drugs: Impact of Drug Structure and Properties on Co-Assembly
    • Hapira, A.; Assaraf, Y. G.; Epstein, D.; Livney, Y. D. Beta-Casein Nanoparticles as an Oral Delivery System for Chemotherapeutic Drugs: Impact of Drug Structure and Properties on Co-Assembly Pharm. Res. 2010, 27, 2175-2186
    • (2010) Pharm. Res. , vol.27 , pp. 2175-2186
    • Hapira, A.1    Assaraf, Y.G.2    Epstein, D.3    Livney, Y.D.4
  • 11
    • 33748322067 scopus 로고    scopus 로고
    • A Review of the Content of the Putative Chemopreventive Phytoalexin Resveratrol in Red Wine
    • Stervbo, U.; Vang, O.; Bonnesen, C. A Review of the Content of the Putative Chemopreventive Phytoalexin Resveratrol in Red Wine Food Chem. 2007, 101, 449-457
    • (2007) Food Chem. , vol.101 , pp. 449-457
    • Stervbo, U.1    Vang, O.2    Bonnesen, C.3
  • 12
    • 33645831366 scopus 로고    scopus 로고
    • Chocolate and Cocoa: New Sources of trans -Resveratrol and trans -Piceid
    • Counet, C.; Callemien, D.; Collin, S. Chocolate and Cocoa: New Sources of trans -Resveratrol and trans -Piceid Food Chem. 2006, 98, 649-657
    • (2006) Food Chem. , vol.98 , pp. 649-657
    • Counet, C.1    Callemien, D.2    Collin, S.3
  • 13
    • 0029867396 scopus 로고    scopus 로고
    • Wines and Grape Juices as Modulators of Platelet Aggregation in Healthy Human Subjects
    • PaceAsciak, C. R.; Rounova, O.; Hahn, S. E.; Diamandis, E. P.; Goldberg, D. M. Wines and Grape Juices as Modulators of Platelet Aggregation in Healthy Human Subjects Clin. Chim. Acta 1996, 246, 163-182
    • (1996) Clin. Chim. Acta , vol.246 , pp. 163-182
    • Paceasciak, C.R.1    Rounova, O.2    Hahn, S.E.3    Diamandis, E.P.4    Goldberg, D.M.5
  • 14
    • 0036307853 scopus 로고    scopus 로고
    • Diparate in vitro and in vivo Antilukeukemic Effects of Resveratrol, a Natural Polyphenolic Compound Found in Grapes
    • Cao, X.; Xu, Y. X.; Divine, G.; Janakiraman, N.; Chapman, R. A.; Gautam, S. C. Diparate in vitro and in vivo Antilukeukemic Effects of Resveratrol, a Natural Polyphenolic Compound Found in Grapes J. Nutr. 2002, 132, 2076-2081
    • (2002) J. Nutr. , vol.132 , pp. 2076-2081
    • Cao, X.1    Xu, Y.X.2    Divine, G.3    Janakiraman, N.4    Chapman, R.A.5    Gautam, S.C.6
  • 15
    • 0036676571 scopus 로고    scopus 로고
    • Resveratrol, a Chemopreventive Agent, Disrupts the Cell Cycle Control of Human SW480 Colorectal Tumor Cells
    • Delmas, D.; Passilly-Degrace, P.; Jannin, B.; Malik, M. C.; Latruffe, N. Resveratrol, a Chemopreventive Agent, Disrupts the Cell Cycle Control of Human SW480 Colorectal Tumor Cells Int. J. Mol. Med. 2002, 10, 193-199
    • (2002) Int. J. Mol. Med. , vol.10 , pp. 193-199
    • Delmas, D.1    Passilly-Degrace, P.2    Jannin, B.3    Malik, M.C.4    Latruffe, N.5
  • 16
    • 0034212162 scopus 로고    scopus 로고
    • DNA Breakage by Resveratrol and Cu(II): Reaction Mechanism and Bacteriophage Inactivation
    • Ahmad, A.; Asad, S. F.; Singh, S.; Hadi, S. M. DNA Breakage by Resveratrol and Cu(II): Reaction Mechanism and Bacteriophage Inactivation Cancer Lett. 2000, 154, 29-37
    • (2000) Cancer Lett. , vol.154 , pp. 29-37
    • Ahmad, A.1    Asad, S.F.2    Singh, S.3    Hadi, S.M.4
  • 17
    • 0027479424 scopus 로고
    • Genistein Arrests Cell Cycle Progression at G2-M
    • Nishino, H.; Aoike, A. Genistein Arrests Cell Cycle Progression at G2-M Cancer Res. 1993, 53, 1328-1331
    • (1993) Cancer Res. , vol.53 , pp. 1328-1331
    • Nishino, H.1    Aoike, A.2
  • 18
    • 0035863857 scopus 로고    scopus 로고
    • Different Effects of Genisten and Resveratrol on Oxidative DNA Damage in Vitro
    • Win, W.; Cao, Z.; Peng, X.; Trush, M. A.; Li, Y. Different Effects of Genisten and Resveratrol on Oxidative DNA Damage in Vitro Mutat. Res. 2002, 513, 113-120
    • (2002) Mutat. Res. , vol.513 , pp. 113-120
    • Win, W.1    Cao, Z.2    Peng, X.3    Trush, M.A.4    Li, Y.5
  • 20
    • 33644901007 scopus 로고    scopus 로고
    • Multiple Biological Activities of Curcumin: A Short Review
    • Maheshwari, R. K.; Singh, A. K.; Gaddipati, J.; Srimal, R. C. Multiple Biological Activities of Curcumin: A Short Review Life Sci. 2006, 78, 2081-2087
    • (2006) Life Sci. , vol.78 , pp. 2081-2087
    • Maheshwari, R.K.1    Singh, A.K.2    Gaddipati, J.3    Srimal, R.C.4
  • 21
    • 34248573808 scopus 로고    scopus 로고
    • Curcumin Potentiates Antitumor Activity of Gemcitabine in an Orthotopic Model of Pancreatic Cancer through Suppression of Proliferation, Angiogenesis, and Inhibition of Nuclear Factor-κB-Regulated Gene Products
    • Kunnumakkara, A. B.; Guha, S.; Krishnan, S.; Diagaradjane, P.; Gelovani, J.; Aggarwal, B. B. Curcumin Potentiates Antitumor Activity of Gemcitabine in an Orthotopic Model of Pancreatic Cancer through Suppression of Proliferation, Angiogenesis, and Inhibition of Nuclear Factor-κB-Regulated Gene Products Cancer Res. 2007, 67, 3853-3861
    • (2007) Cancer Res. , vol.67 , pp. 3853-3861
    • Kunnumakkara, A.B.1    Guha, S.2    Krishnan, S.3    Diagaradjane, P.4    Gelovani, J.5    Aggarwal, B.B.6
  • 22
    • 0028872989 scopus 로고
    • Chemoprevention of Colon Carcinogenesis by Dietary Curcumin, a Naturally Occurring Plant Phenolic Compound
    • Rao, C. V.; Rivenson, A.; Simi, B.; Reddy, B. S. Chemoprevention of Colon Carcinogenesis by Dietary Curcumin, a Naturally Occurring Plant Phenolic Compound Cancer Res. 1995, 55, 259-266
    • (1995) Cancer Res. , vol.55 , pp. 259-266
    • Rao, C.V.1    Rivenson, A.2    Simi, B.3    Reddy, B.S.4
  • 23
    • 66049097051 scopus 로고    scopus 로고
    • Fluorescence Spectral Resolution of Tryptophan Residues in Bovine and Human Serum Albumins
    • Tayeh, N.; Rungassamy, T.; Albani, J. R. Fluorescence Spectral Resolution of Tryptophan Residues in Bovine and Human Serum Albumins J. Pharm. Biomed. Anal. 2009, 50, 107-116
    • (2009) J. Pharm. Biomed. Anal. , vol.50 , pp. 107-116
    • Tayeh, N.1    Rungassamy, T.2    Albani, J.R.3
  • 26
    • 0024622619 scopus 로고
    • On the Spectral Subtraction of Water from the FT-IR Spectra of Aqueous Solutions of Proteins
    • Dousseau, F.; Therrien, M.; Pezolet, M. On the Spectral Subtraction of Water from the FT-IR Spectra of Aqueous Solutions of Proteins Appl. Spectrosc. 1989, 43, 538-542
    • (1989) Appl. Spectrosc. , vol.43 , pp. 538-542
    • Dousseau, F.1    Therrien, M.2    Pezolet, M.3
  • 27
    • 0022691315 scopus 로고
    • Examination of the Secondary Structure of Proteins by Deconvoluted FTIR Spectra
    • Byler, D. M.; Susi, H. Examination of the Secondary Structure of Proteins by Deconvoluted FTIR Spectra Biopolymers 1986, 25, 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 29
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing Protein Circular Dichroism Spectra for Accurate Secondary Structure
    • Johnson, W. C. Analyzing Protein Circular Dichroism Spectra for Accurate Secondary Structure Proteins: Struct., Funct., Genet. 1999, 35, 307-312
    • (1999) Proteins: Struct., Funct., Genet. , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 30
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON and CDSSTR Methods with an Expanded Reference Set
    • Seerama, N.; Woody, R. W. Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON and CDSSTR Methods with an Expanded Reference Set Anal. Biochem. 2000, 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Seerama, N.1    Woody, R.W.2
  • 31
    • 27744522469 scopus 로고    scopus 로고
    • Spectroscopic Studies of the Interaction of Anti-Coagulant Rodenticide Diphacinone with Human Serum Albumin
    • Tang, J.; Qi, S.; Chen, X. Spectroscopic Studies of the Interaction of Anti-Coagulant Rodenticide Diphacinone with Human Serum Albumin J. Mol. Struct. 2005, 779, 87-95
    • (2005) J. Mol. Struct. , vol.779 , pp. 87-95
    • Tang, J.1    Qi, S.2    Chen, X.3
  • 32
    • 70349099296 scopus 로고    scopus 로고
    • Binding of the Scutellarin to Albumin Using Tryptophan Fluorescence Quenching, CD and FT-IR Spectra
    • Tian, J.; Liu, J.; Hu, Z.; Chen, X. Binding of the Scutellarin to Albumin Using Tryptophan Fluorescence Quenching, CD and FT-IR Spectra Am. J. Immunol. 2005, 1, 21-23
    • (2005) Am. J. Immunol. , vol.1 , pp. 21-23
    • Tian, J.1    Liu, J.2    Hu, Z.3    Chen, X.4
  • 33
    • 11844253806 scopus 로고    scopus 로고
    • Flavnoid-Serum Albumin Complexation: Determination of Binding Constants and Binding Sites by Fluorescence Spectroscopy
    • Dufour, C.; Dangles, O. Flavnoid-Serum Albumin Complexation: Determination of Binding Constants and Binding Sites by Fluorescence Spectroscopy Biochim. Biophys. Acta 2005, 1721, 164-173
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 34
    • 3242709482 scopus 로고    scopus 로고
    • Investigation of the Interaction between Flavonoids and Human Serum Albumin
    • Bi, S.; Ding, L.; Tian, Y.; Song, D.; Zhou, X.; Liu, X.; Zhang, H. Investigation of the Interaction between Flavonoids and Human Serum Albumin J. Mol. Struct. 2004, 703, 37-45
    • (2004) J. Mol. Struct. , vol.703 , pp. 37-45
    • Bi, S.1    Ding, L.2    Tian, Y.3    Song, D.4    Zhou, X.5    Liu, X.6    Zhang, H.7
  • 35
    • 13444292204 scopus 로고    scopus 로고
    • Effect of Chinese Medicine Alpinetin on the Structure of Human Serum Albumin
    • He, W.; Li, Y.; Xue, C.; Hu, Z.; Chen, X.; Sheng, F. Effect of Chinese Medicine Alpinetin on the Structure of Human Serum Albumin Bioorg. Med. Chem. 2005, 13, 1837-1845
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 1837-1845
    • He, W.1    Li, Y.2    Xue, C.3    Hu, Z.4    Chen, X.5    Sheng, F.6
  • 36
    • 1842612537 scopus 로고    scopus 로고
    • Spectroscopic Studies on the Interaction of Cinnamic Acid and Its Hydroxyl Derivatives with Human Serum Albumin
    • Jian, M.; Xia, M. X.; Zheng, D.; Liu, Y.; Li, X. Y.; Chen, X. Spectroscopic Studies on the Interaction of Cinnamic Acid and Its Hydroxyl Derivatives with Human Serum Albumin J. Mol. Struct. 2004, 692, 71-80
    • (2004) J. Mol. Struct. , vol.692 , pp. 71-80
    • Jian, M.1    Xia, M.X.2    Zheng, D.3    Liu, Y.4    Li, X.Y.5    Chen, X.6
  • 37
    • 0023008334 scopus 로고
    • Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins
    • Krimm, S.; Bandekar, J. Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins Adv. Protein Chem. 1986, 38, 181-364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 40
    • 0032246954 scopus 로고    scopus 로고
    • Changes in the Secondary Structure of Bovine Casein by Fourier Transform Infrared Spectroscopy: Effects of Calcium and Temperature
    • Curley, D. M.; Kumosinski, T. F.; Unruh, J. J.; Farrell, H. M., Jr. Changes in the Secondary Structure of Bovine Casein by Fourier Transform Infrared Spectroscopy: Effects of Calcium and Temperature J. Dairy Sci. 1998, 81, 3154-3162
    • (1998) J. Dairy Sci. , vol.81 , pp. 3154-3162
    • Curley, D.M.1    Kumosinski, T.F.2    Unruh, J.J.3    Farrell Jr., H.M.4
  • 41
    • 40849116384 scopus 로고    scopus 로고
    • Effect of Surfactants on Casein Structure: A Spectroscopic Study
    • Chokraborty, A.; Basak, S. Effect of Surfactants on Casein Structure: A Spectroscopic Study Colloids Surf., B 2007, 63, 83-90
    • (2007) Colloids Surf., B , vol.63 , pp. 83-90
    • Chokraborty, A.1    Basak, S.2
  • 42
  • 43
    • 0025378934 scopus 로고
    • Structure and Ligand Binding Properties of Human Serum Albumin
    • Kragh-Hansen, U. Structure and Ligand Binding Properties of Human Serum Albumin Dan. Med. Bull. 1990, 37, 57-84
    • (1990) Dan. Med. Bull. , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 45
    • 0034335286 scopus 로고    scopus 로고
    • Effect of Solvent on the Excited-State Photophysical Properties of Curcumin
    • Khopde, S. M.; Prianarsin, K.; Palit, D. K.; Mukherjee, T. Effect of Solvent on the Excited-State Photophysical Properties of Curcumin Photochem. Photobiol. 2000, 72, 625-631
    • (2000) Photochem. Photobiol. , vol.72 , pp. 625-631
    • Khopde, S.M.1    Prianarsin, K.2    Palit, D.K.3    Mukherjee, T.4
  • 46
    • 75649126908 scopus 로고    scopus 로고
    • Study on the Interaction of Cationic Lipids with Bovine Serum Albumin
    • Charbonneau, D.; Tajmir-Riahi, H. A. Study on the Interaction of Cationic Lipids with Bovine Serum Albumin J. Phys. Chem. B 2010, 114, 1148-1155
    • (2010) J. Phys. Chem. B , vol.114 , pp. 1148-1155
    • Charbonneau, D.1    Tajmir-Riahi, H.A.2
  • 47
    • 76249105826 scopus 로고    scopus 로고
    • Complexes of Dendrimers with Bovine Serum Albumin
    • Mandeville, J. S.; Tajmir- Riahi, H. A. Complexes of Dendrimers with Bovine Serum Albumin Biomacromolecules 2010, 11, 465-472
    • (2010) Biomacromolecules , vol.11 , pp. 465-472
    • Mandeville, J.S.1    Tajmir- Riahi, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.