메뉴 건너뛰기




Volumn 95, Issue , 2019, Pages 526-532

Thermodynamic and kinetic study of epigallocatechin-3-gallate-bovine lactoferrin complex formation determined by surface plasmon resonance (SPR): A comparative study with fluorescence spectroscopy

Author keywords

Activated complex; Entropy increasing; Rate constants

Indexed keywords

ASSOCIATION REACTIONS; FLUORESCENCE; KINETICS; MAMMALS; MEDICAL INFORMATION SYSTEMS; RATE CONSTANTS; SURFACE PLASMON RESONANCE; THERMODYNAMICS;

EID: 85065846926     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2019.04.065     Document Type: Article
Times cited : (30)

References (41)
  • 1
    • 85027404480 scopus 로고    scopus 로고
    • Epigallocatechin-3-Gallate: The prospective targeting of cancer stem cells and preventing metastasis of chemically-induced mammary cancer in rats
    • Abd El-Rahman, S.S., Shehab, G., Nashaat, H., Epigallocatechin-3-Gallate: The prospective targeting of cancer stem cells and preventing metastasis of chemically-induced mammary cancer in rats. The American Journal of the Medical Sciences 354:1 (2017), 54–63 https://doi.org/10.1016/J.AMJMS.2017.03.001.
    • (2017) The American Journal of the Medical Sciences , vol.354 , Issue.1 , pp. 54-63
    • Abd El-Rahman, S.S.1    Shehab, G.2    Nashaat, H.3
  • 2
    • 84960800820 scopus 로고    scopus 로고
    • Encapsulation and controlled release of bioactive compounds in lactoferrin-glycomacropeptide nanohydrogels: Curcumin and caffeine as model compounds
    • Bourbon, A.I., Cerqueira, M.A., Vicente, A.A., Encapsulation and controlled release of bioactive compounds in lactoferrin-glycomacropeptide nanohydrogels: Curcumin and caffeine as model compounds. Journal of Food Engineering 180 (2016), 110–119 https://doi.org/10.1016/j.jfoodeng.2016.02.016.
    • (2016) Journal of Food Engineering , vol.180 , pp. 110-119
    • Bourbon, A.I.1    Cerqueira, M.A.2    Vicente, A.A.3
  • 5
    • 84909582948 scopus 로고    scopus 로고
    • Self-assembled micellar nanocomplexes comprising green tea catechin derivatives and protein drugs for cancer therapy
    • Chung, J.E., Tan, S., Gao, S.J., Yongvongsoontorn, N., Kim, S.H., Lee, J.H., Ying, J.Y., Self-assembled micellar nanocomplexes comprising green tea catechin derivatives and protein drugs for cancer therapy. Nature Nanotechnology 9:11 (2014), 907–912 https://doi.org/10.1038/nnano.2014.208.
    • (2014) Nature Nanotechnology , vol.9 , Issue.11 , pp. 907-912
    • Chung, J.E.1    Tan, S.2    Gao, S.J.3    Yongvongsoontorn, N.4    Kim, S.H.5    Lee, J.H.6    Ying, J.Y.7
  • 6
    • 85056204506 scopus 로고    scopus 로고
    • Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and ferulic acid interactions following UHT-like treatment
    • Condict, L., Kaur, J., Hung, A., Ashton, J., Kasapis, S., Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and ferulic acid interactions following UHT-like treatment. Food Hydrocolloids 89 (2019), 351–359 https://doi.org/10.1016/J.FOODHYD.2018.10.055.
    • (2019) Food Hydrocolloids , vol.89 , pp. 351-359
    • Condict, L.1    Kaur, J.2    Hung, A.3    Ashton, J.4    Kasapis, S.5
  • 7
    • 79955018181 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate potently inhibits the in vitro activity of hydroxy-3-methyl-glutaryl-CoA reductase
    • Cuccioloni, M., Mozzicafreddo, M., Spina, M., Tran, C.N., Falconi, M., Eleuteri, A.M., Angeletti, M., Epigallocatechin-3-gallate potently inhibits the in vitro activity of hydroxy-3-methyl-glutaryl-CoA reductase. Journal of Lipid Research 52:5 (2011), 897–907 https://doi.org/10.1194/jlr.M011817.
    • (2011) Journal of Lipid Research , vol.52 , Issue.5 , pp. 897-907
    • Cuccioloni, M.1    Mozzicafreddo, M.2    Spina, M.3    Tran, C.N.4    Falconi, M.5    Eleuteri, A.M.6    Angeletti, M.7
  • 8
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • Day, Y.S.N., Baird, C.L., Rich, R.L., Myszka, D.G., Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods. Protein Science 11 (2002), 1017–1025 https://doi.org/10.1110/ps.4330102.the.
    • (2002) Protein Science , vol.11 , pp. 1017-1025
    • Day, Y.S.N.1    Baird, C.L.2    Rich, R.L.3    Myszka, D.G.4
  • 10
    • 85026863555 scopus 로고    scopus 로고
    • Potential of casein as a carrier for biologically active agents
    • Głąb, T.K., Boratyński, J., Potential of casein as a carrier for biologically active agents. Topics in Current Chemistry, 375(4), 2017 https://doi.org/10.1007/s41061-017-0158-z.
    • (2017) Topics in Current Chemistry , vol.375 , Issue.4
    • Głąb, T.K.1    Boratyński, J.2
  • 11
  • 14
    • 85041691513 scopus 로고    scopus 로고
    • Probing the interaction of two chemotherapeutic drugs of oxali-palladium and 5-fluorouracil simultaneously with milk carrier protein of β-lactoglobulin
    • Leilabadi-Asl, A., Divsalar, A., Saboury, A.A., Parivar, K., Probing the interaction of two chemotherapeutic drugs of oxali-palladium and 5-fluorouracil simultaneously with milk carrier protein of β-lactoglobulin. International Journal of Biological Macromolecules 112 (2018), 422–432 https://doi.org/10.1016/j.ijbiomac.2018.01.067.
    • (2018) International Journal of Biological Macromolecules , vol.112 , pp. 422-432
    • Leilabadi-Asl, A.1    Divsalar, A.2    Saboury, A.A.3    Parivar, K.4
  • 15
    • 85037528856 scopus 로고    scopus 로고
    • Lactoferrin exerts antitumor effects by inhibiting angiogenesis in a HT29 human colon tumor model
    • acs.jafc.7b03390
    • Li, H.-Y., Li, M., Luo, C., Wang, J.-Q., Zheng, N., Lactoferrin exerts antitumor effects by inhibiting angiogenesis in a HT29 human colon tumor model. Journal of Agricultural and Food Chemistry, 2017 acs.jafc.7b03390 https://doi.org/10.1021/acs.jafc.7b03390.
    • (2017) Journal of Agricultural and Food Chemistry
    • Li, H.-Y.1    Li, M.2    Luo, C.3    Wang, J.-Q.4    Zheng, N.5
  • 16
    • 84958955693 scopus 로고    scopus 로고
    • Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH
    • Liu, F., Wang, D., Ma, C., Gao, Y., Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH. Food Hydrocolloids 58 (2016), 49–59 https://doi.org/10.1016/j.foodhyd.2016.02.011.
    • (2016) Food Hydrocolloids , vol.58 , pp. 49-59
    • Liu, F.1    Wang, D.2    Ma, C.3    Gao, Y.4
  • 20
    • 84989352609 scopus 로고    scopus 로고
    • How to distinguish conformational selection and induced fit based on chemical relaxation rates
    • Paul, F., Weikl, T.R., How to distinguish conformational selection and induced fit based on chemical relaxation rates. PLoS Computational Biology 12:9 (2016), 1–17 https://doi.org/10.1371/journal.pcbi.1005067.
    • (2016) PLoS Computational Biology , vol.12 , Issue.9 , pp. 1-17
    • Paul, F.1    Weikl, T.R.2
  • 21
    • 36148980862 scopus 로고    scopus 로고
    • Interactions between flavan-3-ols and poly (L-proline)studied by isothermal titration Calorimetry : Effect of the tannin strucuture
    • Poncet-Legrand, C., Gautier, C., Cheynier, V., Imberty, A., Interactions between flavan-3-ols and poly (L-proline)studied by isothermal titration Calorimetry : Effect of the tannin strucuture. Journal of Agricultural and Food Chemistry 55 (2007), 9235–9240 https://doi.org/10.1021/jf071297o.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 9235-9240
    • Poncet-Legrand, C.1    Gautier, C.2    Cheynier, V.3    Imberty, A.4
  • 22
    • 85061663842 scopus 로고    scopus 로고
    • Comparison of binding interactions of cyanidin-3-O-glucoside to β-conglycinin and glycinin using multi-spectroscopic and thermodynamic methods
    • Ren, C., Xiong, W., Li, J., Li, B., Comparison of binding interactions of cyanidin-3-O-glucoside to β-conglycinin and glycinin using multi-spectroscopic and thermodynamic methods. Food Hydrocolloids 92 (2019), 155–162 https://doi.org/10.1016/J.FOODHYD.2019.01.053.
    • (2019) Food Hydrocolloids , vol.92 , pp. 155-162
    • Ren, C.1    Xiong, W.2    Li, J.3    Li, B.4
  • 23
    • 85028949949 scopus 로고    scopus 로고
    • Lactoferrin-derived peptides active towards influenza: Identification of three potent tetrapeptide inhibitors
    • Scala, M.C., Sala, M., Pietrantoni, A., Spensiero, A., Di Micco, S., Agamennone, M., Campiglia, P., Lactoferrin-derived peptides active towards influenza: Identification of three potent tetrapeptide inhibitors. Scientific Reports, 7(1), 2017, 10593 https://doi.org/10.1038/s41598-017-10492-x.
    • (2017) Scientific Reports , vol.7 , Issue.1 , pp. 10593
    • Scala, M.C.1    Sala, M.2    Pietrantoni, A.3    Spensiero, A.4    Di Micco, S.5    Agamennone, M.6    Campiglia, P.7
  • 25
    • 85021909945 scopus 로고    scopus 로고
    • Epigallocatechin gallate, an active green tea compound inhibits the Zika virus entry into host cells via binding the envelope protein
    • Sharma, N., Murali, A., Singh, S.K., Giri, R., Epigallocatechin gallate, an active green tea compound inhibits the Zika virus entry into host cells via binding the envelope protein. International Journal of Biological Macromolecules 104 (2017), 1046–1054 https://doi.org/10.1016/j.ijbiomac.2017.06.105.
    • (2017) International Journal of Biological Macromolecules , vol.104 , pp. 1046-1054
    • Sharma, N.1    Murali, A.2    Singh, S.K.3    Giri, R.4
  • 28
    • 84921489093 scopus 로고    scopus 로고
    • Beneficial effects of dietary EGCG and voluntary exercise on behavior in an alzheimer's disease mouse model
    • Walker, J.M., Klakotskaia, D., Ajit, D., Weisman, G.A., Wood, W.G., Sun, G.Y., Schachtman, T.R., Beneficial effects of dietary EGCG and voluntary exercise on behavior in an alzheimer's disease mouse model. Journal of Alzheimer's Disease 44:2 (2015), 561–572 https://doi.org/10.3233/JAD-140981.
    • (2015) Journal of Alzheimer's Disease , vol.44 , Issue.2 , pp. 561-572
    • Walker, J.M.1    Klakotskaia, D.2    Ajit, D.3    Weisman, G.A.4    Wood, W.G.5    Sun, G.Y.6    Schachtman, T.R.7
  • 29
    • 84862271632 scopus 로고    scopus 로고
    • Thermodynamic analysis of the molecular interactions between amyloid β-protein fragments and (−)-Epigallocatechin-3-gallate
    • Wang, S.-H., Dong, X.-Y., Sun, Y., Thermodynamic analysis of the molecular interactions between amyloid β-protein fragments and (−)-Epigallocatechin-3-gallate. The Journal of Physical Chemistry B 116:20 (2012), 5803–5809 https://doi.org/10.1021/jp209406t.
    • (2012) The Journal of Physical Chemistry B , vol.116 , Issue.20 , pp. 5803-5809
    • Wang, S.-H.1    Dong, X.-Y.2    Sun, Y.3
  • 30
    • 77956307401 scopus 로고    scopus 로고
    • Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (−)-Epigallocatechin-3-gallate
    • Wang, S.-H., Liu, F.-F., Dong, X.-Y., Sun, Y., Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (−)-Epigallocatechin-3-gallate. The Journal of Physical Chemistry B 114:35 (2010), 11576–11583 https://doi.org/10.1021/jp1001435.
    • (2010) The Journal of Physical Chemistry B , vol.114 , Issue.35 , pp. 11576-11583
    • Wang, S.-H.1    Liu, F.-F.2    Dong, X.-Y.3    Sun, Y.4
  • 31
    • 84862777628 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the interactions between insulin and (-)-epigallocatechin-3-gallate
    • Wang, S.H., Liu, F.F., Dong, X.Y., Sun, Y., Calorimetric and spectroscopic studies of the interactions between insulin and (-)-epigallocatechin-3-gallate. Biochemical Engineering Journal 62 (2012), 70–78 https://doi.org/10.1016/j.bej.2012.01.005.
    • (2012) Biochemical Engineering Journal , vol.62 , pp. 70-78
    • Wang, S.H.1    Liu, F.F.2    Dong, X.Y.3    Sun, Y.4
  • 32
    • 84879794535 scopus 로고    scopus 로고
    • Non-arrhenius protein aggregation
    • Wang, W., Roberts, C.J., Non-arrhenius protein aggregation. The AAPS Journal 15:3 (2013), 840–851 https://doi.org/10.1208/s12248-013-9485-3.
    • (2013) The AAPS Journal , vol.15 , Issue.3 , pp. 840-851
    • Wang, W.1    Roberts, C.J.2
  • 33
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • van de Weert, M., Stella, L., Fluorescence quenching and ligand binding: A critical discussion of a popular methodology. Journal of Molecular Structure 998:1–3 (2011), 144–150 https://doi.org/10.1016/J.MOLSTRUC.2011.05.023.
    • (2011) Journal of Molecular Structure , vol.998 , Issue.1-3 , pp. 144-150
    • van de Weert, M.1    Stella, L.2
  • 34
    • 84884468885 scopus 로고    scopus 로고
    • Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase
    • Wu, X., He, W., Yao, L., Zhang, H., Liu, Z., Wang, W., Cao, J., Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase. Journal of Agricultural and Food Chemistry 61:37 (2013), 8829–8835 https://doi.org/10.1021/jf401779z.
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , Issue.37 , pp. 8829-8835
    • Wu, X.1    He, W.2    Yao, L.3    Zhang, H.4    Liu, Z.5    Wang, W.6    Cao, J.7
  • 35
    • 85032269000 scopus 로고    scopus 로고
    • Epigallocatechin gallate-β-lactoglobulin nanoparticles improve the antitumor activity of EGCG for inducing cancer cell apoptosis
    • Wu, M., Jin, J., Jin, P., Xu, Y., Yin, J., Qin, D., Du, Q., Epigallocatechin gallate-β-lactoglobulin nanoparticles improve the antitumor activity of EGCG for inducing cancer cell apoptosis. Journal of Functional Foods 39 (2017), 257–263 https://doi.org/10.1016/J.JFF.2017.10.038.
    • (2017) Journal of Functional Foods , vol.39 , pp. 257-263
    • Wu, M.1    Jin, J.2    Jin, P.3    Xu, Y.4    Yin, J.5    Qin, D.6    Du, Q.7
  • 36
    • 85030555334 scopus 로고    scopus 로고
    • Epigallocatechin gallate has a neurorescue effect in a mouse model of Parkinson disease
    • Xu, Q., Langley, M., Kanthasamy, A.G., Reddy, M.B., Epigallocatechin gallate has a neurorescue effect in a mouse model of Parkinson disease. Journal of Nutrition 147:10 (2017), 1926–1931 https://doi.org/10.3945/jn.117.255034.
    • (2017) Journal of Nutrition , vol.147 , Issue.10 , pp. 1926-1931
    • Xu, Q.1    Langley, M.2    Kanthasamy, A.G.3    Reddy, M.B.4
  • 37
    • 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., Xu, C., Yuan, F., Gao, Y., Molecular interaction between (-)-epigallocatechin-3-gallate and bovine lactoferrin using multi-spectroscopic method and isothermal titration calorimetry. Food Research International 64 (2014), 141–149 https://doi.org/10.1016/j.foodres.2014.06.001.
    • (2014) Food Research International , vol.64 , pp. 141-149
    • Yang, W.1    Liu, F.2    Xu, C.3    Yuan, F.4    Gao, Y.5
  • 38
    • 67649449180 scopus 로고    scopus 로고
    • Cancer prevention by tea: Animal studies, molecular mechanisms and human relevance
    • Yang, C.S., Wang, X., Lu, G., Picinich, S.C., Cancer prevention by tea: Animal studies, molecular mechanisms and human relevance. Nature Reviews Cancer 9:6 (2009), 429–439 https://doi.org/10.1038/nrc2641.
    • (2009) Nature Reviews Cancer , vol.9 , Issue.6 , pp. 429-439
    • Yang, C.S.1    Wang, X.2    Lu, G.3    Picinich, S.C.4
  • 39
    • 76749084741 scopus 로고    scopus 로고
    • Characterization of binding interactions between green tea flavanoids and milk proteins
    • Yuksel, Z., Avci, E., Erdem, Y.K., Characterization of binding interactions between green tea flavanoids and milk proteins. Food Chemistry 121:2 (2010), 450–456 https://doi.org/10.1016/j.foodchem.2009.12.064.
    • (2010) Food Chemistry , vol.121 , Issue.2 , pp. 450-456
    • Yuksel, Z.1    Avci, E.2    Erdem, Y.K.3
  • 40
    • 85055888849 scopus 로고    scopus 로고
    • Improved antioxidant activity, bioaccessibility and bioavailability of EGCG by delivery in β-lactoglobulin particles
    • Zagury, Y., Kazir, M., Livney, Y.D., Improved antioxidant activity, bioaccessibility and bioavailability of EGCG by delivery in β-lactoglobulin particles. Journal of Functional Foods 52 (2019), 121–130 https://doi.org/10.1016/J.JFF.2018.10.025.
    • (2019) Journal of Functional Foods , vol.52 , pp. 121-130
    • Zagury, Y.1    Kazir, M.2    Livney, Y.D.3
  • 41
    • 84868241407 scopus 로고    scopus 로고
    • Experimental and theoretical studies on the binding of epigallocatechin gallate to puri fi ed porcine gastric mucin
    • Zhao, Y., Chen, L., Yakubov, G., Aminiafshar, T., Han, L., Experimental and theoretical studies on the binding of epigallocatechin gallate to puri fi ed porcine gastric mucin. The Journal of Physical Chemistry B 116 (2012), 13010–13016.
    • (2012) The Journal of Physical Chemistry B , vol.116 , pp. 13010-13016
    • Zhao, Y.1    Chen, L.2    Yakubov, G.3    Aminiafshar, T.4    Han, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.