메뉴 건너뛰기




Volumn 65, Issue 14, 2017, Pages 3019-3030

Formation of a Multiligand Complex of Bovine Serum Albumin with Retinol, Resveratrol, and (-)-Epigallocatechin-3-gallate for the Protection of Bioactive Components

Author keywords

( ) epigallocatechin 3 gallate; bovine serum albumin; complex; resveratrol; retinol

Indexed keywords

BODY FLUIDS; DICHROISM; MAMMALS; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 85030558428     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.7b00326     Document Type: Article
Times cited : (59)

References (45)
  • 2
    • 0034039993 scopus 로고    scopus 로고
    • Ligand-binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands
    • De Wolf, F. A.; Brett, G. M. Ligand-binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands Pharmacol. Rev. 2000, 52, 207-236
    • (2000) Pharmacol. Rev. , vol.52 , pp. 207-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 3
    • 84899906485 scopus 로고    scopus 로고
    • Milk proteins as encapsulation devices and delivery vehicles: Applications and trends
    • Tavares, G. M.; Croguennec, T.; Carvalho, A. F.; Bouhallab, S. Milk proteins as encapsulation devices and delivery vehicles: Applications and trends Trends Food Sci. Technol. 2014, 37, 5-20 10.1016/j.tifs.2014.02.008
    • (2014) Trends Food Sci. Technol. , vol.37 , pp. 5-20
    • Tavares, G.M.1    Croguennec, T.2    Carvalho, A.F.3    Bouhallab, S.4
  • 5
    • 33747602306 scopus 로고    scopus 로고
    • Spectroscopic study of the interaction between folic acid and bovine serum albumin
    • Zhang, A. M.; Jia, L. P. Spectroscopic study of the interaction between folic acid and bovine serum albumin Spectrosc. Lett. 2006, 39, 285-298 10.1080/00387010600779112
    • (2006) Spectrosc. Lett. , vol.39 , pp. 285-298
    • Zhang, A.M.1    Jia, L.P.2
  • 7
    • 66749158582 scopus 로고    scopus 로고
    • Self-assembly of ibuprofen and bovine serum albumin-dextran conjugates leading to effective loading of the drug
    • Li, J.; Yao, P. Self-assembly of ibuprofen and bovine serum albumin-dextran conjugates leading to effective loading of the drug Langmuir 2009, 25, 6385-6391 10.1021/la804288u
    • (2009) Langmuir , vol.25 , pp. 6385-6391
    • Li, J.1    Yao, P.2
  • 8
    • 84882956883 scopus 로고    scopus 로고
    • Biopolymeric Amphiphiles and Their Assemblies as Functional Food Ingredients and Nutraceutical Delivery Systems
    • In; Garti, N. McClements, D. J. Woodhead Publishing: Cambridge, UK
    • Livney, Y. D. Biopolymeric Amphiphiles and Their Assemblies as Functional Food Ingredients and Nutraceutical Delivery Systems. In Encapsulation Technologies and Delivery Systems for Food Ingredients and Nutraceuticals; Garti, N.; McClements, D. J., Eds.; Woodhead Publishing: Cambridge, UK, 2012; pp 252-286.
    • (2012) Encapsulation Technologies and Delivery Systems for Food Ingredients and Nutraceuticals , pp. 252-286
    • Livney, Y.D.1
  • 9
    • 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
  • 10
    • 84155162705 scopus 로고    scopus 로고
    • A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin
    • Roy, A. S.; Tripathy, D. R.; Chatterjee, A.; Dasgupta, S. A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin J. Biophys. Chem. 2010, 1, 141-152 10.4236/jbpc.2010.13017
    • (2010) J. Biophys. Chem. , vol.1 , pp. 141-152
    • Roy, A.S.1    Tripathy, D.R.2    Chatterjee, A.3    Dasgupta, S.4
  • 11
    • 84865339163 scopus 로고    scopus 로고
    • Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking
    • Skrt, M.; Benedik, E.; Podlipnik, C.; Ulrih, N. P. Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking Food Chem. 2012, 135, 2418-2424 10.1016/j.foodchem.2012.06.114
    • (2012) Food Chem. , vol.135 , pp. 2418-2424
    • Skrt, M.1    Benedik, E.2    Podlipnik, C.3    Ulrih, N.P.4
  • 12
    • 84856023397 scopus 로고    scopus 로고
    • Binding sites of retinol and retinoic acid with serum albumins
    • Belatik, A.; Hotchandani, S.; Bariyanga, J.; Tajmir-Riahi, H. A. Binding sites of retinol and retinoic acid with serum albumins Eur. J. Med. Chem. 2012, 48, 114-123 10.1016/j.ejmech.2011.12.002
    • (2012) Eur. J. Med. Chem. , vol.48 , pp. 114-123
    • Belatik, A.1    Hotchandani, S.2    Bariyanga, J.3    Tajmir-Riahi, H.A.4
  • 13
    • 84903466140 scopus 로고    scopus 로고
    • Molecular interaction between (-)-epigallocatechin-3-gallate and bovine lactoferrin using multi-spectroscopic method and isothermal titration calorimetry
    • Yang, W.; Liu, F. G.; Xu, C. Q.; Yuan, F.; Gao, Y. X. Molecular interaction between (-)-epigallocatechin-3-gallate and bovine lactoferrin using multi-spectroscopic method and isothermal titration calorimetry Food Res. Int. 2014, 64, 141-149 10.1016/j.foodres.2014.06.001
    • (2014) Food Res. Int. , vol.64 , pp. 141-149
    • Yang, W.1    Liu, F.G.2    Xu, C.Q.3    Yuan, F.4    Gao, Y.X.5
  • 14
    • 84979782486 scopus 로고    scopus 로고
    • Binding to bovine serum albumin protects β-carotene against oxidative degradation
    • Chang, H. T.; Cheng, H.; Han, R. M.; Zhang, J. P.; Skibsted, L. H. Binding to bovine serum albumin protects β-carotene against oxidative degradation J. Agric. Food Chem. 2016, 64, 5951-5957 10.1021/acs.jafc.6b02436
    • (2016) J. Agric. Food Chem. , vol.64 , pp. 5951-5957
    • Chang, H.T.1    Cheng, H.2    Han, R.M.3    Zhang, J.P.4    Skibsted, L.H.5
  • 15
    • 84943172673 scopus 로고    scopus 로고
    • Interaction of tea polyphenols with serum albumins: A fluorescence spectroscopic analysis
    • Bose, A. Interaction of tea polyphenols with serum albumins: A fluorescence spectroscopic analysis J. Lumin. 2016, 169, 220-226 10.1016/j.jlumin.2015.09.018
    • (2016) J. Lumin. , vol.169 , pp. 220-226
    • Bose, A.1
  • 16
    • 33745610160 scopus 로고    scopus 로고
    • Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: Fluorescence, fourier transform infrared, circular dichroism, and docking studies
    • Maiti, T. K.; Ghosh, K. S.; Dasgupta, S. Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: Fluorescence, fourier transform infrared, circular dichroism, and docking studies Proteins: Struct., Funct., Genet. 2006, 64, 355-362 10.1002/prot.20995
    • (2006) Proteins: Struct., Funct., Genet. , vol.64 , pp. 355-362
    • Maiti, T.K.1    Ghosh, K.S.2    Dasgupta, S.3
  • 17
    • 34447337251 scopus 로고    scopus 로고
    • Investigation of adsorption behavior of (-)-epigallocatechin gallate on bovine serum albumin surface using quartz crystal microbalance with dissipation monitoring
    • Wang, X. Y.; Ho, C. T.; Huang, Q. R. Investigation of adsorption behavior of (-)-epigallocatechin gallate on bovine serum albumin surface using quartz crystal microbalance with dissipation monitoring J. Agric. Food Chem. 2007, 55, 4987-4992 10.1021/jf070590l
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 4987-4992
    • Wang, X.Y.1    Ho, C.T.2    Huang, Q.R.3
  • 18
  • 20
    • 43049108788 scopus 로고    scopus 로고
    • The scavenging capacity and synergistic effects of lycopene, vitamin E, vitamin C, and beta-carotene mixtures on the DPPH free radical
    • Liu, D. H.; Shi, J.; Ibarra, A. C.; Kakuda, Y.; Xue, S. J. The scavenging capacity and synergistic effects of lycopene, vitamin E, vitamin C, and beta-carotene mixtures on the DPPH free radical Lwt-Food Science and Technology 2008, 41, 1344-1349 10.1016/j.lwt.2007.08.001
    • (2008) Lwt-Food Science and Technology , vol.41 , pp. 1344-1349
    • Liu, D.H.1    Shi, J.2    Ibarra, A.C.3    Kakuda, Y.4    Xue, S.J.5
  • 21
    • 85075095162 scopus 로고    scopus 로고
    • 1187 Molecular mechanism of synergistic anti-tumor activity by the combination of natural compounds green tea (-)-epigallocathetin-3-gallate (EGCG) and resveratrol for potential chemoprevention in head and neck cancer (HNC)
    • Shin, D. M.; Amin, A. R. M.; Wang, D.; Rahman, M. A.; Nannapaneni, S.; Khuri, F. R.; Chen, Z. G. 1187 Molecular mechanism of synergistic anti-tumor activity by the combination of natural compounds green tea (-)-epigallocathetin-3-gallate (EGCG) and resveratrol for potential chemoprevention in head and neck cancer (HNC) Eur. J. Cancer 2012, 48, S286 10.1016/S0959-8049(12)71781-1
    • (2012) Eur. J. Cancer , vol.48 , pp. S286
    • Shin, D.M.1    Amin, A.R.M.2    Wang, D.3    Rahman, M.A.4    Nannapaneni, S.5    Khuri, F.R.6    Chen, Z.G.7
  • 23
    • 84902673717 scopus 로고    scopus 로고
    • A study of multi-ligand beta-lactoglobulin complex formation
    • Zhang, J.; Liu, X. M.; Subirade, M.; Zhou, P.; Liang, L. A study of multi-ligand beta-lactoglobulin complex formation Food Chem. 2014, 165, 256-261 10.1016/j.foodchem.2014.05.109
    • (2014) Food Chem. , vol.165 , pp. 256-261
    • Zhang, J.1    Liu, X.M.2    Subirade, M.3    Zhou, P.4    Liang, L.5
  • 24
    • 79961134868 scopus 로고    scopus 로고
    • Investigation on the interaction between ilaprazole and bovine serum albumin without or with different C-Ring flavonoids from the viewpoint of food-drug interference
    • Zhang, Y. P.; Shi, S. Y.; Chen, X. Q.; Zhang, W.; Huang, K. L.; Peng, M. J. Investigation on the interaction between ilaprazole and bovine serum albumin without or with different C-Ring flavonoids from the viewpoint of food-drug interference J. Agric. Food Chem. 2011, 59, 8499-8506 10.1021/jf201796x
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 8499-8506
    • Zhang, Y.P.1    Shi, S.Y.2    Chen, X.Q.3    Zhang, W.4    Huang, K.L.5    Peng, M.J.6
  • 25
    • 84857059676 scopus 로고    scopus 로고
    • Study of the acid and thermal stability of beta-lactoglobulin-ligand complexes using fluorescence quenching
    • Liang, L.; Subirade, M. Study of the acid and thermal stability of beta-lactoglobulin-ligand complexes using fluorescence quenching Food Chem. 2012, 132, 2023-2029 10.1016/j.foodchem.2011.12.043
    • (2012) Food Chem. , vol.132 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 27
    • 34547683463 scopus 로고    scopus 로고
    • Automatic perception of organic molecules based on essential structural information
    • Zhao, Y.; Cheng, T. J.; Wang, R. X. Automatic perception of organic molecules based on essential structural information J. Chem. Inf. Model. 2007, 47, 1379-1385 10.1021/ci700028w
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 1379-1385
    • Zhao, Y.1    Cheng, T.J.2    Wang, R.X.3
  • 28
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • Trott, O.; Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading J. Comput. Chem. 2010, 31, 455-461 10.1002/jcc.21334
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 29
    • 77953325845 scopus 로고    scopus 로고
    • Ligand docking and binding site analysis with PyMOL and Autodock/Vina
    • Seeliger, D.; de Groot, B. L. Ligand docking and binding site analysis with PyMOL and Autodock/Vina J. Comput.-Aided Mol. Des. 2010, 24, 417-422 10.1007/s10822-010-9352-6
    • (2010) J. Comput.-Aided Mol. Des. , vol.24 , pp. 417-422
    • Seeliger, D.1    De Groot, B.L.2
  • 30
    • 46149098431 scopus 로고    scopus 로고
    • Probing the interaction of trans-resveratrol with bovine serum albumin: A fluorescence quenching study with Tachiya model
    • Xiao, J. B.; Chen, X. Q.; Jiang, X. Y.; Hilczer, M.; Tachiya, M. Probing the interaction of trans-resveratrol with bovine serum albumin: A fluorescence quenching study with Tachiya model J. Fluoresc. 2008, 18, 671-678 10.1007/s10895-008-0346-x
    • (2008) J. Fluoresc. , vol.18 , pp. 671-678
    • Xiao, J.B.1    Chen, X.Q.2    Jiang, X.Y.3    Hilczer, M.4    Tachiya, M.5
  • 31
    • 68749092038 scopus 로고    scopus 로고
    • Interaction between trans-resveratrol and serum albumin in aqueous solution
    • Cao, S. H.; Wang, D. D.; Tan, X. Y.; Chen, J. W. Interaction between trans-resveratrol and serum albumin in aqueous solution J. Solution Chem. 2009, 38, 1193-1202 10.1007/s10953-009-9439-7
    • (2009) J. Solution Chem. , vol.38 , pp. 1193-1202
    • Cao, S.H.1    Wang, D.D.2    Tan, X.Y.3    Chen, J.W.4
  • 33
    • 84993999426 scopus 로고    scopus 로고
    • Competitive binding of (-)-epigallocatechin-3-gallate and 5-fluorouracil to human serum albumin: A fluorescence and circular dichroism study
    • Yuan, L. X.; Liu, M.; Liu, G. Q.; Li, D. C.; Wang, Z. P.; Wang, B. Q.; Han, J.; Zhang, M. Competitive binding of (-)-epigallocatechin-3-gallate and 5-fluorouracil to human serum albumin: A fluorescence and circular dichroism study Spectrochim. Acta, Part A 2017, 173, 584-592 10.1016/j.saa.2016.10.023
    • (2017) Spectrochim. Acta, Part A , vol.173 , pp. 584-592
    • Yuan, L.X.1    Liu, M.2    Liu, G.Q.3    Li, D.C.4    Wang, Z.P.5    Wang, B.Q.6    Han, J.7    Zhang, M.8
  • 34
    • 59849124286 scopus 로고    scopus 로고
    • Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods
    • Zhang, Y. Z.; Zhou, B.; Zhang, X. P.; Huang, P.; Li, C. H.; Liu, Y. Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods J. Hazard. Mater. 2009, 163, 1345-1352 10.1016/j.jhazmat.2008.07.132
    • (2009) J. Hazard. Mater. , vol.163 , pp. 1345-1352
    • Zhang, Y.Z.1    Zhou, B.2    Zhang, X.P.3    Huang, P.4    Li, C.H.5    Liu, Y.6
  • 35
    • 84963647545 scopus 로고    scopus 로고
    • Spectrofluorimetric and molecular docking investigation on the interaction of 6-azauridine, a pyrimidine nucleoside antimetabolite, with serum protein
    • Uppuluri, K. B.; Ahmed, K. B. A.; Jothi, A.; Veerappan, A. Spectrofluorimetric and molecular docking investigation on the interaction of 6-azauridine, a pyrimidine nucleoside antimetabolite, with serum protein J. Mol. Liq. 2016, 219, 602-607 10.1016/j.molliq.2016.02.102
    • (2016) J. Mol. Liq. , vol.219 , pp. 602-607
    • Uppuluri, K.B.1    Ahmed, K.B.A.2    Jothi, A.3    Veerappan, A.4
  • 37
    • 0015523573 scopus 로고
    • The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, beta-lactoglobulin, and the retinol-binding protein of human plasma
    • Futterman, S.; Heller, J. The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, beta-lactoglobulin, and the retinol-binding protein of human plasma J. Biol. Chem. 1972, 247, 5168-5172
    • (1972) J. Biol. Chem. , vol.247 , pp. 5168-5172
    • Futterman, S.1    Heller, J.2
  • 38
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of beta-Lactoglobulin with resveratrol and its biological implications
    • Liang, L.; Tajmir-Riahi, H. A.; Subirade, M. Interaction of beta-Lactoglobulin with resveratrol and its biological implications Biomacromolecules 2008, 9, 50-56 10.1021/bm700728k
    • (2008) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 40
    • 0347026133 scopus 로고    scopus 로고
    • Stabilization of all-trans-retinol by cyclodextrins: A comparative study using HPLC and fluorescence spectroscopy
    • Semenova, E. M.; Cooper, A.; Wilson, C. G.; Converse, C. A. Stabilization of all-trans-retinol by cyclodextrins: A comparative study using HPLC and fluorescence spectroscopy J. Inclusion Phenom. Mol. Recognit. Chem. 2002, 44, 155-158 10.1023/A:1023042612880
    • (2002) J. Inclusion Phenom. Mol. Recognit. Chem. , vol.44 , pp. 155-158
    • Semenova, E.M.1    Cooper, A.2    Wilson, C.G.3    Converse, C.A.4
  • 41
    • 84857517864 scopus 로고    scopus 로고
    • Effects of green tea catechin on the lipid oxidation, volatile compound formation, and losses of retinol and alpha-tocopherol in whole milk during light illumination as compared with ascorbic acid
    • Jung, M. Y. Effects of green tea catechin on the lipid oxidation, volatile compound formation, and losses of retinol and alpha-tocopherol in whole milk during light illumination as compared with ascorbic acid Food Sci. Biotechnol. 2011, 20, 1425-1434 10.1007/s10068-011-0196-1
    • (2011) Food Sci. Biotechnol. , vol.20 , pp. 1425-1434
    • Jung, M.Y.1
  • 42
    • 84928502779 scopus 로고    scopus 로고
    • Stability and solubility of trans-resveratrol are strongly influenced by pH and temperature
    • Zupancic, S.; Lavric, Z.; Kristl, J. Stability and solubility of trans-resveratrol are strongly influenced by pH and temperature Eur. J. Pharm. Biopharm. 2015, 93, 196-204 10.1016/j.ejpb.2015.04.002
    • (2015) Eur. J. Pharm. Biopharm. , vol.93 , pp. 196-204
    • Zupancic, S.1    Lavric, Z.2    Kristl, J.3
  • 43
    • 80052966488 scopus 로고    scopus 로고
    • Activation energy of light induced isomerization of resveratrol
    • Figueiras, T. S.; Neves-Petersen, M. T.; Petersen, S. B. Activation energy of light induced isomerization of resveratrol J. Fluoresc. 2011, 21, 1897-1906 10.1007/s10895-011-0886-3
    • (2011) J. Fluoresc. , vol.21 , pp. 1897-1906
    • Figueiras, T.S.1    Neves-Petersen, M.T.2    Petersen, S.B.3
  • 44
    • 84871551534 scopus 로고    scopus 로고
    • Kinetic study of catechin stability: Effects of pH, concentration, and temperature
    • Li, N.; Taylor, L. S.; Ferruzzi, M. G.; Mauer, L. J. Kinetic study of catechin stability: Effects of pH, concentration, and temperature J. Agric. Food Chem. 2012, 60, 12531-12539 10.1021/jf304116s
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 12531-12539
    • Li, N.1    Taylor, L.S.2    Ferruzzi, M.G.3    Mauer, L.J.4
  • 45
    • 0042622256 scopus 로고    scopus 로고
    • Stability of tea theaflavins and catechins
    • Su, Y. L.; Leung, L. K.; Huang, Y.; Chen, Z. Y. Stability of tea theaflavins and catechins Food Chem. 2003, 83, 189-195 10.1016/S0308-8146(03)00062-1
    • (2003) Food Chem. , vol.83 , pp. 189-195
    • Su, Y.L.1    Leung, L.K.2    Huang, Y.3    Chen, Z.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.