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Volumn 8, Issue 1, 2014, Pages 331-339

Studies on the interaction of naringin palmitate with lysozyme by spectroscopic analysis

Author keywords

Fluorescence spectroscopy; Interaction; Lysozyme; Naringin; Naringin palmitate

Indexed keywords


EID: 84899981163     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2014.03.026     Document Type: Article
Times cited : (17)

References (40)
  • 4
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • Dufour C., Dangles O. Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy. Biochimica et Biophysica Acta General Subjects 2005, 1721:164-173.
    • (2005) Biochimica et Biophysica Acta General Subjects , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 6
    • 38649127868 scopus 로고    scopus 로고
    • Spectrophotometric studies on the interaction between (-)-epigallocatechin gallate and lysozyme
    • Ghosh K.S., Sahoo B.K., Dasgupta S. Spectrophotometric studies on the interaction between (-)-epigallocatechin gallate and lysozyme. Chemical Physics Letters 2008, 452:193-197.
    • (2008) Chemical Physics Letters , vol.452 , pp. 193-197
    • Ghosh, K.S.1    Sahoo, B.K.2    Dasgupta, S.3
  • 8
    • 33750176864 scopus 로고    scopus 로고
    • Comparison of the characterization on binding of alpinetin and cardamonin to lysozyme by spectroscopic methods
    • He W., Li Y., Tang J., Luan F., Jin J., Hu Z. Comparison of the characterization on binding of alpinetin and cardamonin to lysozyme by spectroscopic methods. International Journal of Biological Macromolecules 2006, 39:165-173.
    • (2006) International Journal of Biological Macromolecules , vol.39 , pp. 165-173
    • He, W.1    Li, Y.2    Tang, J.3    Luan, F.4    Jin, J.5    Hu, Z.6
  • 9
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
    • Hu Y.J., Liu Y., Pi Z.B., Qu S.S. Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study. Bioorganic & Medicinal Chemistry 2005, 13:6609-6614.
    • (2005) Bioorganic & Medicinal Chemistry , vol.13 , pp. 6609-6614
    • Hu, Y.J.1    Liu, Y.2    Pi, Z.B.3    Qu, S.S.4
  • 12
    • 0036148318 scopus 로고    scopus 로고
    • Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin
    • Klajnert B., Bryszewska M. Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin. Bioelectrochemistry (Amsterdam, Netherlands) 2002, 55:33-35.
    • (2002) Bioelectrochemistry (Amsterdam, Netherlands) , vol.55 , pp. 33-35
    • Klajnert, B.1    Bryszewska, M.2
  • 14
    • 0019073217 scopus 로고
    • Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies
    • Lakowicz J.R., Freshwater G., Weber G. Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies. Biophysical Journal 1980, 32:591-601.
    • (1980) Biophysical Journal , vol.32 , pp. 591-601
    • Lakowicz, J.R.1    Freshwater, G.2    Weber, G.3
  • 15
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz J.R., Weber G. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 1973, 12:4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 17
    • 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 2007, 9:50-56.
    • (2007) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 18
    • 77953480879 scopus 로고    scopus 로고
    • Antioxidant properties of modified rutin esters by DPPH, reducing power, iron chelation and human low density lipoprotein assays
    • Lue B.M., Nielsen N.S., Jacobsen C., Hellgren L., Guo Z., Xu X. Antioxidant properties of modified rutin esters by DPPH, reducing power, iron chelation and human low density lipoprotein assays. Food Chemistry 2010, 123:221-230.
    • (2010) Food Chemistry , vol.123 , pp. 221-230
    • Lue, B.M.1    Nielsen, N.S.2    Jacobsen, C.3    Hellgren, L.4    Guo, Z.5    Xu, X.6
  • 19
    • 13544259806 scopus 로고    scopus 로고
    • Biocatalytic preparation of acylated derivatives of flavonoid glycosides enhances their antioxidant and antimicrobial activity
    • Mellou F., Lazari D., Skaltsa H., Tselepis A.D., Kolisis F.N., Stamatis H. Biocatalytic preparation of acylated derivatives of flavonoid glycosides enhances their antioxidant and antimicrobial activity. Journal of Biotechnology 2005, 116:295-304.
    • (2005) Journal of Biotechnology , vol.116 , pp. 295-304
    • Mellou, F.1    Lazari, D.2    Skaltsa, H.3    Tselepis, A.D.4    Kolisis, F.N.5    Stamatis, H.6
  • 20
    • 0001749712 scopus 로고
    • Recent developments in fluorescence and chemiluminescence analysis. Plenary lecture
    • Miller J.N. Recent developments in fluorescence and chemiluminescence analysis. Plenary lecture. The Analyst 1984, 109:191-198.
    • (1984) The Analyst , vol.109 , pp. 191-198
    • Miller, J.N.1
  • 24
    • 0027491794 scopus 로고
    • Study of interaction of carprofen and its enantiomers with human serum albumin - I. Mechanism of binding studied by dialysis and spectroscopic methods
    • Rahman M.H., Maruyama T., Okada T., Yamasaki K., Otagiri M. Study of interaction of carprofen and its enantiomers with human serum albumin - I. Mechanism of binding studied by dialysis and spectroscopic methods. Biochemical Pharmacology 1993, 46:1721-1731.
    • (1993) Biochemical Pharmacology , vol.46 , pp. 1721-1731
    • Rahman, M.H.1    Maruyama, T.2    Okada, T.3    Yamasaki, K.4    Otagiri, M.5
  • 25
    • 33748413614 scopus 로고    scopus 로고
    • Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence
    • Rawel H.M., Frey S.K., Meidtner K., Kroll J., Schweigert F.J. Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence. Molecular Nutrition & Food Research 2006, 50:705-713.
    • (2006) Molecular Nutrition & Food Research , vol.50 , pp. 705-713
    • Rawel, H.M.1    Frey, S.K.2    Meidtner, K.3    Kroll, J.4    Schweigert, F.J.5
  • 26
    • 77957020511 scopus 로고    scopus 로고
    • Antifungal activity of natural and enzymatically-modified flavonoids isolated from citrus species
    • Salas M.P., Céliz G., Geronazzo H., Daz M., Resnik S.L. Antifungal activity of natural and enzymatically-modified flavonoids isolated from citrus species. Food Chemistry 2011, 124:1411-1415.
    • (2011) Food Chemistry , vol.124 , pp. 1411-1415
    • Salas, M.P.1    Céliz, G.2    Geronazzo, H.3    Daz, M.4    Resnik, S.L.5
  • 28
    • 5044238048 scopus 로고    scopus 로고
    • Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method
    • Tian J.N., Liu J.Q., He W.Y., Hu Z.D., Yao X.J., Chen X.G. Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules 2004, 5:1956-1961.
    • (2004) Biomacromolecules , vol.5 , pp. 1956-1961
    • Tian, J.N.1    Liu, J.Q.2    He, W.Y.3    Hu, Z.D.4    Yao, X.J.5    Chen, X.G.6
  • 29
    • 80052964795 scopus 로고    scopus 로고
    • Binding of quercetin to lysozyme as probed by spectroscopic analysis and molecular simulation
    • Wang G., Wang L., Tang W., Hao X.X., Wang Y., Lu Y. Binding of quercetin to lysozyme as probed by spectroscopic analysis and molecular simulation. Journal of Fluorescence 2011, 21:1879-1886.
    • (2011) Journal of Fluorescence , vol.21 , pp. 1879-1886
    • Wang, G.1    Wang, L.2    Tang, W.3    Hao, X.X.4    Wang, Y.5    Lu, Y.6
  • 30
    • 34247399095 scopus 로고    scopus 로고
    • Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study
    • Wang Y.Q., Zhang H.M., Zhang G.C., Tao W.H., Tang S.H. Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study. Journal of Luminescence 2007, 126:211-218.
    • (2007) Journal of Luminescence , vol.126 , pp. 211-218
    • Wang, Y.Q.1    Zhang, H.M.2    Zhang, G.C.3    Tao, W.H.4    Tang, S.H.5
  • 34
    • 67649248246 scopus 로고    scopus 로고
    • Studies on the interaction of lysozyme with naringein and naringin by fluorescence spectroscopy
    • Yang R., Qu L., Chen X., Li J., Li P. Studies on the interaction of lysozyme with naringein and naringin by fluorescence spectroscopy. Acta Chimica Sinica-Chinese Edition 2006, 64:1349-1354.
    • (2006) Acta Chimica Sinica-Chinese Edition , vol.64 , pp. 1349-1354
    • Yang, R.1    Qu, L.2    Chen, X.3    Li, J.4    Li, P.5
  • 35
    • 84869496013 scopus 로고    scopus 로고
    • The interaction of flavonoid-lysozyme and the relationship between molecular structure of flavonoids and their binding activity to lysozyme
    • Yang R., Yu L., Zeng H., Liang R., Chen X., Qu L. The interaction of flavonoid-lysozyme and the relationship between molecular structure of flavonoids and their binding activity to lysozyme. Journal of Fluorescence 2012, 22:1449-1459.
    • (2012) Journal of Fluorescence , vol.22 , pp. 1449-1459
    • Yang, R.1    Yu, L.2    Zeng, H.3    Liang, R.4    Chen, X.5    Qu, L.6
  • 37
    • 84875166973 scopus 로고    scopus 로고
    • Investigation of the interaction of naringin palmitate with bovine serum albumin. Spectroscopic analysis and molecular docking
    • Zhang X., Li L., Xu Z.B., Liang Z.L., Su J.Y., Huang J.R., Li B. Investigation of the interaction of naringin palmitate with bovine serum albumin. Spectroscopic analysis and molecular docking. PLoS ONE 2013, 8:e59106.
    • (2013) PLoS ONE , vol.8
    • Zhang, X.1    Li, L.2    Xu, Z.B.3    Liang, Z.L.4    Su, J.Y.5    Huang, J.R.6    Li, B.7
  • 38
    • 84857690392 scopus 로고    scopus 로고
    • Protective effects of epigallocatechin gallate (EGCG) derivatives on azoxymethane-induced colonic carcinogenesis in mice
    • Zhong Y., Chiou Y.S., Pan M.H., Ho C.T., Shahidi F. Protective effects of epigallocatechin gallate (EGCG) derivatives on azoxymethane-induced colonic carcinogenesis in mice. Journal of Functional Foods 2012, 4(1):323-330.
    • (2012) Journal of Functional Foods , vol.4 , Issue.1 , pp. 323-330
    • Zhong, Y.1    Chiou, Y.S.2    Pan, M.H.3    Ho, C.T.4    Shahidi, F.5
  • 39
    • 84857690952 scopus 로고    scopus 로고
    • Antioxidant and antiviral activities of lipophilic epigallocatechin gallate (EGCG) derivatives
    • Zhong Y., Ma C.M., Shahidi F. Antioxidant and antiviral activities of lipophilic epigallocatechin gallate (EGCG) derivatives. Journal of Functional Foods 2012, 4(1):87-93.
    • (2012) Journal of Functional Foods , vol.4 , Issue.1 , pp. 87-93
    • Zhong, Y.1    Ma, C.M.2    Shahidi, F.3
  • 40
    • 79959261640 scopus 로고    scopus 로고
    • Lipophilized epigallocatechin gallate (EGCG) derivatives as novel antioxidants
    • Zhong Y., Shahidi F. Lipophilized epigallocatechin gallate (EGCG) derivatives as novel antioxidants. Journal of Agricultural and Food Chemistry 2011, 59(12):6526-6533.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , Issue.12 , pp. 6526-6533
    • Zhong, Y.1    Shahidi, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.