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Volumn 56, Issue 5, 2010, Pages 331-334

Influence of the galloyl moiety in tea catechins on binding affinity for human serum albumin

Author keywords

Binding affinity; Catechin; Galloyl moiety; Galloyl moietycatechin; Human serum albumin; Interaction

Indexed keywords

EPICATECHIN; EPICATECHIN GALLATE; EPIGALLOCATECHIN; EPIGALLOCATECHIN GALLATE; HUMAN SERUM ALBUMIN; PHOSPHATE;

EID: 78651499242     PISSN: 03014800     EISSN: 18817742     Source Type: Journal    
DOI: 10.3177/jnsv.56.331     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 9744244998 scopus 로고    scopus 로고
    • A review of the health effects of green tea catechins in vivo animal models
    • Crespy V, Williamson G. 2004. A review of the health effects of green tea catechins in vivo animal models. J Nutr 134: 3431S-3440S.
    • (2004) J Nutr , vol.134
    • Crespy, V.1    Williamson, G.2
  • 2
    • 33644645034 scopus 로고    scopus 로고
    • Beneficial effects of tea and its polyphenols against prostate cancer
    • Siddiqui IA, Adhami VM, Saleem M, Mukhtar H. 2006. Beneficial effects of tea and its polyphenols against prostate cancer. Mol Nutr Food Res 50: 130-143.
    • (2006) Mol Nutr Food Res , vol.50 , pp. 130-143
    • Siddiqui, I.A.1    Adhami, V.M.2    Saleem, M.3    Mukhtar, H.4
  • 3
    • 0034027493 scopus 로고    scopus 로고
    • Scavenging effect of tea catechins and their epimers on superoxide anion radicals generated by a hypoxanthine and xanthine oxidase system
    • Unno T, Sugimoto A, Kakuda K. 2000. Scavenging effect of tea catechins and their epimers on superoxide anion radicals generated by a hypoxanthine and xanthine oxidase system. J Sci Food Agric 80: 601-606.
    • (2000) J Sci Food Agric , vol.80 , pp. 601-606
    • Unno, T.1    Sugimoto, A.2    Kakuda, K.3
  • 4
    • 49449098176 scopus 로고    scopus 로고
    • Nongallated compared with gallated flavan-3-ols in green and black tea are more bioavailable
    • Henning SM, Choo JJ, Heber D. 2008. Nongallated compared with gallated flavan-3-ols in green and black tea are more bioavailable. J Nutr 138: 1529S-1534S.
    • (2008) J Nutr , vol.138
    • Henning, S.M.1    Choo, J.J.2    Heber, D.3
  • 5
    • 0032779295 scopus 로고    scopus 로고
    • In vitro and in vivo activities of tea catechins against Helicobacter pylori
    • Mabe K, Yamada M, Oguni I, Takahashi T. 1999. In vitro and in vivo activities of tea catechins against Helicobacter pylori. Antimicrob Agents Chemother 43: 1788-1791.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1788-1791
    • Mabe, K.1    Yamada, M.2    Oguni, I.3    Takahashi, T.4
  • 6
    • 27644518720 scopus 로고    scopus 로고
    • Antiviral effect of catechins in green tea on influenza virus
    • Song JM, Lee KH, Seong BL. 2005. Antiviral effect of catechins in green tea on influenza virus. Antiviral Res 68: 66-74.
    • (2005) Antiviral Res , vol.68 , pp. 66-74
    • Song, J.M.1    Lee, K.H.2    Seong, B.L.3
  • 7
    • 67649449180 scopus 로고    scopus 로고
    • Cancer prevention by tea: Animal studies, molecular mechanisms and human relevance
    • Yang CS, Wang X, Lu G, Picinich SC. 2009. Cancer prevention by tea: animal studies, molecular mechanisms and human relevance. Nat Rev Cancer 9: 429-439.
    • (2009) Nat Rev Cancer , vol.9 , pp. 429-439
    • Yang, C.S.1    Wang, X.2    Lu, G.3    Picinich, S.C.4
  • 8
    • 0242298292 scopus 로고    scopus 로고
    • The galloyl moiety of green tea catechins is the critical structural feature to inhibit fatty-acid synthase
    • Wang X, Song KS, Guo QX, Tian WX. 2003. The galloyl moiety of green tea catechins is the critical structural feature to inhibit fatty-acid synthase. Biochem Pharmacol 66: 2039-2047.
    • (2003) Biochem Pharmacol , vol.66 , pp. 2039-2047
    • Wang, X.1    Song, K.S.2    Guo, Q.X.3    Tian, W.X.4
  • 11
    • 70350237026 scopus 로고    scopus 로고
    • Catechol type polyphenol is a potential modifier of protein sulfhydryls: Development and application of a new probe for understanding the dietary polyphenol actions
    • Ishii T, Ishikawa M, Miyoshi N, Yasunaga M, Akagawa M, Uchida K, Nakamura Y. 2009. Catechol type polyphenol is a potential modifier of protein sulfhydryls: development and application of a new probe for understanding the dietary polyphenol actions. Chem Res Toxicol 22: 1689-1698.
    • (2009) Chem Res Toxicol , vol.22 , pp. 1689-1698
    • Ishii, T.1    Ishikawa, M.2    Miyoshi, N.3    Yasunaga, M.4    Akagawa, M.5    Uchida, K.6    Nakamura, Y.7
  • 12
    • 34548051331 scopus 로고    scopus 로고
    • Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary -amylase (HSA) by fluorescence quenching
    • Soares S, Mateus N, Freitas V. 2007. Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary -amylase (HSA) by fluorescence quenching. J Agric Food Chem 55: 6726-6735.
    • (2007) J Agric Food Chem , vol.55 , pp. 6726-6735
    • Soares, S.1    Mateus, N.2    Freitas, V.3
  • 13
    • 61449110165 scopus 로고    scopus 로고
    • Interaction of polyphenols with proteins: Binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism
    • Nozaki A, Hori M, Kimura T, Ito H, Hatano T. 2009. Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism. Chem Pharm Bull 57: 224-228.
    • (2009) Chem Pharm Bull , vol.57 , pp. 224-228
    • Nozaki, A.1    Hori, M.2    Kimura, T.3    Ito, H.4    Hatano, T.5
  • 17
    • 33845230898 scopus 로고    scopus 로고
    • Direct observation of substrate-enzyme complexation by surface forces measurement
    • Suzuki T, Zhang YW, Koyama T, Sasaki DY, Kurihara K. 2006. Direct observation of substrate-enzyme complexation by surface forces measurement. J Am Chem Soc 128: 15209-15214.
    • (2006) J Am Chem Soc , vol.128 , pp. 15209-15214
    • Suzuki, T.1    Zhang, Y.W.2    Koyama, T.3    Sasaki, D.Y.4    Kurihara, K.5
  • 18
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Kragh-Hansen U. 1990. Structure and ligand binding properties of human serum albumin. Dan Med Bull 37: 57-84.
    • (1990) Dan Med Bull , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 20
    • 33745610160 scopus 로고    scopus 로고
    • Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: Fluorescence, fourier transform infrared, circular dichroism, and docking studies
    • Maiti TK, Ghosh KS, Dasgupta S. 2006. Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: fluorescence, fourier transform infrared, circular dichroism, and docking studies. Proteins 64: 355-362.
    • (2006) Proteins , vol.64 , pp. 355-362
    • Maiti, T.K.1    Ghosh, K.S.2    Dasgupta, S.3
  • 21
    • 38049036354 scopus 로고    scopus 로고
    • Interfacial interactions of pectin with bovine serum albumin studied by quartz crystal microbalance with dissipation monitoring: Effect of ionic strength
    • Wang X, Ruengruglikit C, Wang YW, Huang Q. 2007. Interfacial interactions of pectin with bovine serum albumin studied by quartz crystal microbalance with dissipation monitoring: effect of ionic strength. J Agric Food Chem 55: 10425-10431.
    • (2007) J Agric Food Chem , vol.55 , pp. 10425-10431
    • Wang, X.1    Ruengruglikit, C.2    Wang, Y.W.3    Huang, Q.4
  • 22
    • 70349177534 scopus 로고    scopus 로고
    • Interaction of polyphenols with proteins: Binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism
    • Nozaki A, Hori M, Kimura T, Ito H, Hatano T. 2009. Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism. Chem Pharm Bull 57: 1019-1023.
    • (2009) Chem Pharm Bull , vol.57 , pp. 1019-1023
    • Nozaki, A.1    Hori, M.2    Kimura, T.3    Ito, H.4    Hatano, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.