메뉴 건너뛰기




Volumn 187-188, Issue , 2014, Pages 33-42

Exploring binding properties of naringenin with bovine β- lactoglobulin: A fluorescence, molecular docking and molecular dynamics simulation study

Author keywords

Lactoglobulin; Binding parameter; Fluorescence quenching; Molecular modeling; Naringenin

Indexed keywords

BINDING PARAMETER; FLUORESCENCE QUENCHING; MOLECULAR MODELING; NARINGENIN; Β-LACTOGLOBULIN;

EID: 84893687795     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2014.01.003     Document Type: Article
Times cited : (54)

References (45)
  • 1
    • 0029867672 scopus 로고    scopus 로고
    • Flavonoids - Chemistry, metabolism, cardioprotective effects, and dietary sources
    • DOI 10.1016/0955-2863(95)00168-9
    • N. Cook, and S. Samman Flavonoids - chemistry, metabolism, cardioprotective effects, and dietary sources J. Nutr. Biochem. 7 1996 66 76 (Pubitemid 26086316)
    • (1996) Journal of Nutritional Biochemistry , vol.7 , Issue.2 , pp. 66-76
    • Cook, N.C.1    Samman, S.2
  • 2
    • 0036774226 scopus 로고    scopus 로고
    • Flavonoid antioxidants: Chemistry, metabolism and structure-activity relationships
    • DOI 10.1016/S0955-2863(02)00208-5, PII S0955286302002085
    • K.E. Heim, A.R. Tagliaferro, and D.J. Bobilya Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships J. Nutr. Biochem. 13 2002 572 584 (Pubitemid 35246546)
    • (2002) Journal of Nutritional Biochemistry , vol.13 , Issue.10 , pp. 572-584
    • Heim, K.E.1    Tagliaferro, A.R.2    Bobilya, D.J.3
  • 3
    • 0033637140 scopus 로고    scopus 로고
    • The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
    • E. Middleton, C. Kandaswami, and T.C. Theoharides The effects of plant flavonoids on mammalian cells: implications for inflammation, heart disease, and cancer Pharmacol. Rev. 52 2000 673 751
    • (2000) Pharmacol. Rev. , vol.52 , pp. 673-751
    • Middleton, E.1    Kandaswami, C.2    Theoharides, T.C.3
  • 4
    • 33745331668 scopus 로고    scopus 로고
    • Protective role of flavonoids in cardiovascular diseases
    • M. Nandave, S. Ojha, and D. Arya Protective role of flavonoids in cardiovascular diseases Nat. Prod. Radiance 4 2005 166 176
    • (2005) Nat. Prod. Radiance , vol.4 , pp. 166-176
    • Nandave, M.1    Ojha, S.2    Arya, D.3
  • 5
    • 33845282451 scopus 로고
    • Quantitative survey of narirutin, naringin, hesperidin, and neohesperidin in citrus
    • R.L. Rouseff, S.F. Martin, and C.O. Youtsey Quantitative survey of narirutin, naringin, hesperidin, and neohesperidin in citrus J. Agric. Food Chem. 35 1987 1027 1030
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 1027-1030
    • Rouseff, R.L.1    Martin, S.F.2    Youtsey, C.O.3
  • 6
    • 47949087932 scopus 로고    scopus 로고
    • Synthesis, characterization, antioxidant activity and DNA-binding studies of two rare earth(III) complexes with naringenin-2-hydroxy benzoyl hydrazone ligand
    • T.-R. Li, Z.-Y. Yang, B.-D. Wang, and D.-D. Qin Synthesis, characterization, antioxidant activity and DNA-binding studies of two rare earth(III) complexes with naringenin-2-hydroxy benzoyl hydrazone ligand Eur. J. Med. Chem. 43 2008 1688 1695
    • (2008) Eur. J. Med. Chem. , vol.43 , pp. 1688-1695
    • Li, T.-R.1    Yang, Z.-Y.2    Wang, B.-D.3    Qin, D.-D.4
  • 7
    • 13844281685 scopus 로고    scopus 로고
    • Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies
    • C. Manach, G. Williamson, C. Morand, A. Scalbert, and C. Rémésy Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies Am. J. Clin. Nutr. 81 2005 230S 242S
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Manach, C.1    Williamson, G.2    Morand, C.3    Scalbert, A.4    Rémésy, C.5
  • 8
    • 77952531665 scopus 로고    scopus 로고
    • β-Lactoglobulin/folic acid complexes: Formation, characterization, and biological implication
    • L. Liang, and M. Subirade β-Lactoglobulin/folic acid complexes: formation, characterization, and biological implication J. Phys. Chem. B 114 2010 6707 6712
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6707-6712
    • Liang, L.1    Subirade, M.2
  • 9
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with resveratrol and its biological implications
    • L. Liang, H. Tajmir-Riahi, and M. Subirade Interaction of β-lactoglobulin with resveratrol and its biological implications Biomacromolecules 9 2007 50 56
    • (2007) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.2    Subirade, M.3
  • 10
    • 84877080943 scopus 로고    scopus 로고
    • Interactions of β-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids
    • A. Mensi, Y. Choiset, H. Rabesona, T. Haertlé, P. Borel, and J.-M. Chobert Interactions of β-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids J. Agric. Food Chem. 61 2013 4114 4119
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 4114-4119
    • Mensi, A.1    Choiset, Y.2    Rabesona, H.3    Haertlé, T.4    Borel, P.5    Chobert, J.-M.6
  • 11
    • 84863362068 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques
    • G. Zhang, L. Wang, and J. 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.1    Wang, L.2    Pan, J.3
  • 12
    • 80053996719 scopus 로고    scopus 로고
    • Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique
    • S. Bi, L. Yan, B. Pang, and Y. Wang Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique J. Lumin. 132 2012 132 140
    • (2012) J. Lumin. , vol.132 , pp. 132-140
    • Bi, S.1    Yan, L.2    Pang, B.3    Wang, Y.4
  • 13
    • 77955227349 scopus 로고    scopus 로고
    • Characterize the interaction between naringenin and bovine serum albumin using spectroscopic approach
    • Y.-J. Hu, Y. Wang, Y. Ou-Yang, J. Zhou, and Y. Liu Characterize the interaction between naringenin and bovine serum albumin using spectroscopic approach J. Lumin. 130 2010 1394 1399
    • (2010) J. Lumin. , vol.130 , pp. 1394-1399
    • Hu, Y.-J.1    Wang, Y.2    Ou-Yang, Y.3    Zhou, J.4    Liu, Y.5
  • 14
    • 84875166973 scopus 로고    scopus 로고
    • Investigation of the interaction of naringin palmitate with bovine serum albumin: Spectroscopic analysis and molecular docking
    • X. Zhang, L. Li, Z. Xu, Z. Liang, J. Su, J. Huang, and B. Li Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking PLoS One 8 2013 e59106
    • (2013) PLoS One , vol.8 , pp. 59106
    • Zhang, X.1    Li, L.2    Xu, Z.3    Liang, Z.4    Su, J.5    Huang, J.6    Li, B.7
  • 15
    • 84882407570 scopus 로고    scopus 로고
    • A combined spectroscopic, molecular docking and molecular dynamic study on the interaction of quercetin with β-casein nanoparticles
    • F. Mehranfar, A.-K. Bordbar, and H. Parastar A combined spectroscopic, molecular docking and molecular dynamic study on the interaction of quercetin with β-casein nanoparticles J. Photochem. Photobiol. B Biol 127 2013 100 107
    • (2013) J. Photochem. Photobiol. B Biol , vol.127 , pp. 100-107
    • Mehranfar, F.1    Bordbar, A.-K.2    Parastar, H.3
  • 16
    • 84873453386 scopus 로고    scopus 로고
    • Binding sites of resveratrol, genistein, and curcumin with milk α-and β-caseins
    • P. Bourassa, J. Bariyanga, and H.A. Tajmir-Riahi Binding sites of resveratrol, genistein, and curcumin with milk α-and β-caseins J. Phys. Chem. B 117 2013 1287 1295
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1287-1295
    • Bourassa, P.1    Bariyanga, J.2    Tajmir-Riahi, H.A.3
  • 18
    • 80155155891 scopus 로고    scopus 로고
    • Interaction of dietary polyphenols with bovine milk proteins: Molecular structure-affinity relationship and influencing bioactivity aspects
    • J. Xiao, F. Mao, F. Yang, Y. Zhao, C. Zhang, and K. Yamamoto Interaction of dietary polyphenols with bovine milk proteins: Molecular structure-affinity relationship and influencing bioactivity aspects Mol. Nutr. Food Res. 55 2011 1637 1645
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1637-1645
    • Xiao, J.1    Mao, F.2    Yang, F.3    Zhao, Y.4    Zhang, C.5    Yamamoto, K.6
  • 19
    • 0028176030 scopus 로고
    • β-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy
    • E. Dufour, C. Genot, and T. Haertlé β-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1205 1994 105 112
    • (1994) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. , vol.1205 , pp. 105-112
    • Dufour, E.1    Genot, C.2    Haertlé, T.3
  • 21
    • 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
  • 22
    • 1842612537 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin
    • J. Min, X. Meng-Xia, Z. Dong, L. Yuan, L. Xiao-Yu, and C. Xing Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin J. Mol. Struct. 692 2004 71 80
    • (2004) J. Mol. Struct. , vol.692 , pp. 71-80
    • Min, J.1    Meng-Xia, X.2    Dong, Z.3    Yuan, L.4    Xiao-Yu, L.5    Xing, C.6
  • 29
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. Van Der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 30
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • S. Nosé A molecular dynamics method for simulations in the canonical ensemble Mol. Phys. 52 1984 255 268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nosé, S.1
  • 31
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695
    • (1985) Phys. Rev. A , vol.31 , pp. 1695
    • Hoover, W.G.1
  • 32
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single crystals: a new molecular dynamics method J. Appl. Phys. 52 1981 7182
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182
    • Parrinello, M.1    Rahman, A.2
  • 33
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log (N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N·log (N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 35
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • W.R. Ware Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process J. Phys. Chem. 66 1962 455 458
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 36
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 1981 3096 3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 37
    • 33644596182 scopus 로고    scopus 로고
    • Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148
    • S. Roufik, S.F. Gauthier, X. Leng, and S.L. Turgeon Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148 Biomacromolecules 7 2006 419 426
    • (2006) Biomacromolecules , vol.7 , pp. 419-426
    • Roufik, S.1    Gauthier, S.F.2    Leng, X.3    Turgeon, S.L.4
  • 38
    • 0034849396 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: Nonlinear quenching effects related to protein - Protein association
    • DOI 10.1021/jf0012188
    • S. Muresan, A. van der Bent, and F.A. de Wolf Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: nonlinear quenching effects related to protein-protein association J. Agric. Food Chem. 49 2001 2609 2618 (Pubitemid 32843298)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.5 , pp. 2609-2618
    • Muresan, S.1    Van Bent, A.D.2    De Wolf, F.A.3
  • 39
    • 0345313659 scopus 로고    scopus 로고
    • β-Lactoglobulin binds palmitate within its central cavity
    • DOI 10.1074/jbc.274.1.170
    • S.-Y. Wu, M.D. Pérez, P. Puyol, and L. Sawyer β-Lactoglobulin binds palmitate within its central cavity J. Biol. Chem. 274 1999 170 174 (Pubitemid 29035045)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 170-174
    • Wu, S.-Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 40
    • 0025609431 scopus 로고
    • β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites
    • E. Dufour, M.C. Marden, and T. Haertlé β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites FEBS Lett. 277 1990 223 226
    • (1990) FEBS Lett. , vol.277 , pp. 223-226
    • Dufour, E.1    Marden, M.C.2    Haertlé, T.3
  • 42
    • 0019331472 scopus 로고
    • Spectroscopic characterization of β-lactoglobulin-retinol complex
    • R.D. Fugate, and P.-S. Song Spectroscopic characterization of β-lactoglobulin-retinol complex Biochim. Biophys. Acta Protein Struct. 625 1980 28 42
    • (1980) Biochim. Biophys. Acta Protein Struct. , vol.625 , pp. 28-42
    • Fugate, R.D.1    Song, P.-S.2
  • 43
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogenâ€bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogenâ€bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.