메뉴 건너뛰기




Volumn 92, Issue 9, 2007, Pages 3178-3194

Single GUV method reveals interaction of tea catechin (2)-epigallocatechin gallate with lipid membranes

Author keywords

[No Author keywords available]

Indexed keywords

CALCEIN; CATECHIN; EPIGALLOCATECHIN GALLATE; MACROGOL; PHOSPHATIDYLCHOLINE;

EID: 34247626376     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.097105     Document Type: Article
Times cited : (138)

References (47)
  • 1
    • 0024814929 scopus 로고
    • Antibacterial substances in Japanese green tea extract against Streptococcus mutans, a cariogenic bacterium
    • Sakanaka, S., M. Kim, M. Taniguchi, and T. Yamamoto. 1989. Antibacterial substances in Japanese green tea extract against Streptococcus mutans, a cariogenic bacterium. Agric. Biol. Chem. 53:2307-2311.
    • (1989) Agric. Biol. Chem , vol.53 , pp. 2307-2311
    • Sakanaka, S.1    Kim, M.2    Taniguchi, M.3    Yamamoto, T.4
  • 2
    • 0028694401 scopus 로고
    • Antibacterial activity of epigallocatechin gallate against methicillin-resistant Staphylococcus aureus
    • Kono, K., I. Tatara, S. Takeda, K. Arakawa, and Y. Hara. 1994. Antibacterial activity of epigallocatechin gallate against methicillin-resistant Staphylococcus aureus. Kansenshogaku Zasshi. 68:1518-1522.
    • (1994) Kansenshogaku Zasshi , vol.68 , pp. 1518-1522
    • Kono, K.1    Tatara, I.2    Takeda, S.3    Arakawa, K.4    Hara, Y.5
  • 3
    • 0032779295 scopus 로고    scopus 로고
    • In vitro and in vivo activities of tea catechins against Helicobacter pylori
    • Mabe, K., M. Yamada, I. Oguni, and T. Takahashi. 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
  • 4
    • 0034496540 scopus 로고    scopus 로고
    • Tea flavonoids: Their functions, utilization and analysis
    • Wang, H., G. J. Provan, and K. Helliwell. 2000. Tea flavonoids: their functions, utilization and analysis. Trends Food Sci. Tech. 11:152-160.
    • (2000) Trends Food Sci. Tech , vol.11 , pp. 152-160
    • Wang, H.1    Provan, G.J.2    Helliwell, K.3
  • 5
    • 0030582664 scopus 로고    scopus 로고
    • Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes
    • Guo, Q., B. Zhao, M. Li, S. Shen, and W. Xin. 1996. Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes. Biochim. Biophys. Acta. 1304:210-222.
    • (1996) Biochim. Biophys. Acta , vol.1304 , pp. 210-222
    • Guo, Q.1    Zhao, B.2    Li, M.3    Shen, S.4    Xin, W.5
  • 6
    • 0033785598 scopus 로고    scopus 로고
    • Antioxidative activity of green tea treated with radical inhibitor 2,2′-azobis(2- amidinopropane) dihydrochloride
    • Yokozawa, T., E. J. Cho, Y. Hara, and K. Kitani. 2000. Antioxidative activity of green tea treated with radical inhibitor 2,2′-azobis(2- amidinopropane) dihydrochloride. J. Agric. Food Chem. 48:5068-5073.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 5068-5073
    • Yokozawa, T.1    Cho, E.J.2    Hara, Y.3    Kitani, K.4
  • 7
    • 0034910451 scopus 로고    scopus 로고
    • A novel method of measuring hydroxyl radical-scavenging activity of antioxidants using gamma-irradiation
    • Yoshioka, H., Y. Ohashi, M. Akaboshi, Y. Senba, and H. Yoshioka. 2001. A novel method of measuring hydroxyl radical-scavenging activity of antioxidants using gamma-irradiation. Free Radic. Res. 35:265-271.
    • (2001) Free Radic. Res , vol.35 , pp. 265-271
    • Yoshioka, H.1    Ohashi, Y.2    Akaboshi, M.3    Senba, Y.4    Yoshioka, H.5
  • 9
    • 0030941215 scopus 로고    scopus 로고
    • Sealing effects of (-)-epigallocatechin gallate on protein kinase C and protein phosphatase 2A
    • Kitano, K., K. Y. Nam, S. Kimura, H. Fujiki, and Y. Imanishi. 1997. Sealing effects of (-)-epigallocatechin gallate on protein kinase C and protein phosphatase 2A. Biophys. Chem. 65:157-164.
    • (1997) Biophys. Chem , vol.65 , pp. 157-164
    • Kitano, K.1    Nam, K.Y.2    Kimura, S.3    Fujiki, H.4    Imanishi, Y.5
  • 10
    • 0035752067 scopus 로고    scopus 로고
    • Steric effects on interaction of tea catechins with lipid bilayers
    • Kajiya, K., S. Kumazawa, and T. Nakayama. 2001. Steric effects on interaction of tea catechins with lipid bilayers. Biosci. Biotechnol. Biochem. 65:2638-2643.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 2638-2643
    • Kajiya, K.1    Kumazawa, S.2    Nakayama, T.3
  • 11
    • 0037443719 scopus 로고    scopus 로고
    • The relationship between the antioxidant and the antibacterial properties of galloylated catechins and the structure of phospholipid model membranes
    • Caturla, N., E. Vera-Samper, J. Villalain, R. Mateo, and V. Micol. 2003. The relationship between the antioxidant and the antibacterial properties of galloylated catechins and the structure of phospholipid model membranes. Free Rad. Biol. Med. 34:648-662.
    • (2003) Free Rad. Biol. Med , vol.34 , pp. 648-662
    • Caturla, N.1    Vera-Samper, E.2    Villalain, J.3    Mateo, R.4    Micol, V.5
  • 12
    • 1642290918 scopus 로고    scopus 로고
    • Relationship between antibacterial activity of (+)-catechin derivatives and their interaction with a model membrane
    • Kajiya, K., H. Hojo, M. Suzuki, F. Nanjo, S. Kumazawa, and T. Nakayama. 2004. Relationship between antibacterial activity of (+)-catechin derivatives and their interaction with a model membrane. J. Agric. Food Chem. 52:1514-1519.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1514-1519
    • Kajiya, K.1    Hojo, H.2    Suzuki, M.3    Nanjo, F.4    Kumazawa, S.5    Nakayama, T.6
  • 13
    • 4644277726 scopus 로고    scopus 로고
    • Direct evidence of interaction of a green tea polyphenol, epigallocatechin gallate, with lipid bilayers by solid-state nuclear magnetic resonance
    • Kumazawa, S., K. Kajiya, A. Naito, H. Saito, S. Tsuji, M. Tanio, M. Suzuki, F. Nanjo, E. Suzuki, and T. Nakayama. 2004. Direct evidence of interaction of a green tea polyphenol, epigallocatechin gallate, with lipid bilayers by solid-state nuclear magnetic resonance. Biosci. Biotechnol. Biochem. 68:1743-1747.
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , pp. 1743-1747
    • Kumazawa, S.1    Kajiya, K.2    Naito, A.3    Saito, H.4    Tsuji, S.5    Tanio, M.6    Suzuki, M.7    Nanjo, F.8    Suzuki, E.9    Nakayama, T.10
  • 14
    • 33344457290 scopus 로고    scopus 로고
    • Interaction of (+)-catechin with a lipid bilayer studied by the spin probe method
    • Yoshioka, H., H. Haga, M. Kubota, Y. Sakai, and H. Yoshioka. 2006. Interaction of (+)-catechin with a lipid bilayer studied by the spin probe method. Biosci. Biotechnol. Biochem. 70:395-400.
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 395-400
    • Yoshioka, H.1    Haga, H.2    Kubota, M.3    Sakai, Y.4    Yoshioka, H.5
  • 15
    • 11944258697 scopus 로고
    • Entropy-driven tension and bending elasticity in condensed-fluid membranes
    • Evans, E., and E. Rawicz. 1990. Entropy-driven tension and bending elasticity in condensed-fluid membranes. Phys. Rev. Lett. 64:2094-2097.
    • (1990) Phys. Rev. Lett , vol.64 , pp. 2094-2097
    • Evans, E.1    Rawicz, E.2
  • 16
    • 0026651919 scopus 로고
    • Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids
    • Farge, E., and P. F. Devaux. 1992. Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids. Biophys. J. 61:347-357.
    • (1992) Biophys. J , vol.61 , pp. 347-357
    • Farge, E.1    Devaux, P.F.2
  • 18
    • 0035856661 scopus 로고    scopus 로고
    • Giant liposome as a biochemical reactor: Transcription of DNA and transportation by laser tweezers
    • Tsumoto, K., S. Nomura, Y. Nakatani, and K. Yoshikawa. 2001. Giant liposome as a biochemical reactor: transcription of DNA and transportation by laser tweezers. Langmuir. 17:7225-7228.
    • (2001) Langmuir , vol.17 , pp. 7225-7228
    • Tsumoto, K.1    Nomura, S.2    Nakatani, Y.3    Yoshikawa, K.4
  • 20
    • 0037059160 scopus 로고    scopus 로고
    • Shape changes of giant unilamellar vesicles of phosphatidylcholine induced by a de novo designed peptide interacting with their membrane interface
    • Yamashita, Y., S. M. Masum, T. Tanaka, and M. Yamazaki. 2002. Shape changes of giant unilamellar vesicles of phosphatidylcholine induced by a de novo designed peptide interacting with their membrane interface. Langmuir. 18:9638-9641.
    • (2002) Langmuir , vol.18 , pp. 9638-9641
    • Yamashita, Y.1    Masum, S.M.2    Tanaka, T.3    Yamazaki, M.4
  • 21
    • 85121161443 scopus 로고    scopus 로고
    • Yamazaki, M., and Y. Tamba. 2005. The single GUV method for probing biomembrane structure and function. e-J. Surf. Sci. Nanotech. 3:218-227.
    • Yamazaki, M., and Y. Tamba. 2005. The single GUV method for probing biomembrane structure and function. e-J. Surf. Sci. Nanotech. 3:218-227.
  • 23
    • 8344256585 scopus 로고    scopus 로고
    • Shape changes and vesicle fission of giant unilamellar vesicles of liquid-ordered phase membrane induced by lysophosphatidyl-choline
    • Tanaka, T., R. Sano, Y. Yamashita, and M. Yamazaki. 2004. Shape changes and vesicle fission of giant unilamellar vesicles of liquid-ordered phase membrane induced by lysophosphatidyl-choline. Langmuir. 20:9526-9534.
    • (2004) Langmuir , vol.20 , pp. 9526-9534
    • Tanaka, T.1    Sano, R.2    Yamashita, Y.3    Yamazaki, M.4
  • 24
    • 0025044566 scopus 로고
    • Deformation and instability in membrane structure of phospholipid vesicles caused by osmophobic association: Mechanical stress model for the mechanism of poly(ethylene glycol)-induced membrane fusion
    • Yamazaki, M., and T. Ito. 1990. Deformation and instability in membrane structure of phospholipid vesicles caused by osmophobic association: mechanical stress model for the mechanism of poly(ethylene glycol)-induced membrane fusion. Biochemistry. 29:1309-1314.
    • (1990) Biochemistry , vol.29 , pp. 1309-1314
    • Yamazaki, M.1    Ito, T.2
  • 25
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry. 34:6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 27
    • 28544437689 scopus 로고    scopus 로고
    • Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability
    • Tamba, Y., and M. Yamazaki. 2005. Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability. Biochemistry. 44:15823-15833.
    • (2005) Biochemistry , vol.44 , pp. 15823-15833
    • Tamba, Y.1    Yamazaki, M.2
  • 28
    • 0037066601 scopus 로고    scopus 로고
    • A new method for preparation of giant liposomes in high salt concentrations and growth of protein microcrystals in them
    • Yamashita, Y., M. Oka, T. Tanaka, and M. Yamazaki. 2002. A new method for preparation of giant liposomes in high salt concentrations and growth of protein microcrystals in them. Biochim. Biophys. Acta. 1561:129-134.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 129-134
    • Yamashita, Y.1    Oka, M.2    Tanaka, T.3    Yamazaki, M.4
  • 29
    • 0037663875 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Bethesda, MD
    • Rasband, W. S. 1997-2006. Image J. U.S. National Institutes of Health, Bethesda, MD. http://rsb.info.nih.gov/ij/.
    • (1997) Image J
    • Rasband, W.S.1
  • 30
    • 0032517063 scopus 로고    scopus 로고
    • Intermembrane distance in multilamellar vesicles of phosphatidylcholine depends on the interaction free energy between solvents and the hydrophilic segments of the membrane surface
    • Kinoshita, K., S. Furuike, and M. Yamazaki. 1998. Intermembrane distance in multilamellar vesicles of phosphatidylcholine depends on the interaction free energy between solvents and the hydrophilic segments of the membrane surface. Biophys. Chem. 74:237-249.
    • (1998) Biophys. Chem , vol.74 , pp. 237-249
    • Kinoshita, K.1    Furuike, S.2    Yamazaki, M.3
  • 31
    • 0032851749 scopus 로고    scopus 로고
    • Low pH induces an interdigitated gel to bilayer gel phase transition in dihexadecylphosphatidylcholine membrane
    • Furuike, S., V. G. Levadny, S. J. Li, and M. Yamazaki. 1999. Low pH induces an interdigitated gel to bilayer gel phase transition in dihexadecylphosphatidylcholine membrane. Biophys. J. 77:2015-2023.
    • (1999) Biophys. J , vol.77 , pp. 2015-2023
    • Furuike, S.1    Levadny, V.G.2    Li, S.J.3    Yamazaki, M.4
  • 32
    • 0034896576 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on phase stability of cubic phases of membranes of monoolein/dioleoylphosphatidic acid mixture
    • Li, S. J., Y. Yamashita, and M. Yamazaki. 2001. Effect of electrostatic interactions on phase stability of cubic phases of membranes of monoolein/dioleoylphosphatidic acid mixture. Biophys. J. 81:983-993.
    • (2001) Biophys. J , vol.81 , pp. 983-993
    • Li, S.J.1    Yamashita, Y.2    Yamazaki, M.3
  • 33
    • 0000238191 scopus 로고
    • Nonaxisymmetric vesicle shapes in a generalized bilayer-couple model and the transition between oblate and prolate axisymmetric shapes
    • Heinrich, V., S. Svetina, and B. Zeks. 1993. Nonaxisymmetric vesicle shapes in a generalized bilayer-couple model and the transition between oblate and prolate axisymmetric shapes. Phys. Rev. E. 48:3112-3123.
    • (1993) Phys. Rev. E , vol.48 , pp. 3112-3123
    • Heinrich, V.1    Svetina, S.2    Zeks, B.3
  • 34
    • 33846363469 scopus 로고
    • Budding transitions of fluid-bilayer vesicles: The effect of area-difference elasticity
    • Miao, L., U. Seifert, M. Wortis, and H.-G. Döbereiner. 1994. Budding transitions of fluid-bilayer vesicles: the effect of area-difference elasticity. Phys. Rev. E. 49:5389-5407.
    • (1994) Phys. Rev. E , vol.49 , pp. 5389-5407
    • Miao, L.1    Seifert, U.2    Wortis, M.3    Döbereiner, H.-G.4
  • 35
    • 0029750734 scopus 로고    scopus 로고
    • The interaction of polyphenols with bilayers: Conditions for increasing bilayer adhesion
    • Huh, N.-W., N. A. Porter, T. J. McIntosh, and S. A. Simon. 1996. The interaction of polyphenols with bilayers: conditions for increasing bilayer adhesion. Biophys. J. 71:3261-3277.
    • (1996) Biophys. J , vol.71 , pp. 3261-3277
    • Huh, N.-W.1    Porter, N.A.2    McIntosh, T.J.3    Simon, S.A.4
  • 36
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 37
    • 0038242872 scopus 로고    scopus 로고
    • Effect of de novo designed peptides interacting with the lipid-membrane interface on the stability of the cubic phases of the monoolein membrane
    • Masum, S. M., S. J. Li, Y. Tamba, Y. Yamashita, T. Tanaka, and M. Yamazaki. 2003. Effect of de novo designed peptides interacting with the lipid-membrane interface on the stability of the cubic phases of the monoolein membrane. Langmuir. 19:4745-4753.
    • (2003) Langmuir , vol.19 , pp. 4745-4753
    • Masum, S.M.1    Li, S.J.2    Tamba, Y.3    Yamashita, Y.4    Tanaka, T.5    Yamazaki, M.6
  • 38
    • 21844477032 scopus 로고    scopus 로고
    • Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes
    • Lopez-Montero, I., N. Rodriguez, S. Cribier, A. Pohl, M. Velez, and P. F. Devaux. 2005. Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes. J. Biol. Chem. 280:25811-25819.
    • (2005) J. Biol. Chem , vol.280 , pp. 25811-25819
    • Lopez-Montero, I.1    Rodriguez, N.2    Cribier, S.3    Pohl, A.4    Velez, M.5    Devaux, P.F.6
  • 39
    • 0000381573 scopus 로고
    • Generic interaction of flexible membranes
    • R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam
    • Lipowsky, R. 1995. Generic interaction of flexible membranes. In Structure and Dynamics of Membranes. R. Lipowsky and E. Sackmann, editors. Elsevier, Amsterdam.
    • (1995) Structure and Dynamics of Membranes
    • Lipowsky, R.1
  • 40
    • 0030051845 scopus 로고    scopus 로고
    • Shape change and physical properties of giant phospholipid vesicles prepared in the presence of an AC electric field
    • Mathivet, L., S. Cribier, and P. F. Devaux. 1996. Shape change and physical properties of giant phospholipid vesicles prepared in the presence of an AC electric field. Biophys. J. 70:1112-1121.
    • (1996) Biophys. J , vol.70 , pp. 1112-1121
    • Mathivet, L.1    Cribier, S.2    Devaux, P.F.3
  • 42
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation
    • Wenk, M. R., and J. Seelig. 1998. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry. 37:3909-3916.
    • (1998) Biochemistry , vol.37 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 44
    • 20744453382 scopus 로고    scopus 로고
    • Effect of positively charged short peptides on stability of cubic phases of monoolein/dioleoylphosphatidic acid mixtures
    • Masum, S. M., S. J. Li, T. S. Awad, and M. Yamazaki. 2005. Effect of positively charged short peptides on stability of cubic phases of monoolein/dioleoylphosphatidic acid mixtures. Langmuir. 21:5290-5297.
    • (2005) Langmuir , vol.21 , pp. 5290-5297
    • Masum, S.M.1    Li, S.J.2    Awad, T.S.3    Yamazaki, M.4
  • 45
    • 0035370113 scopus 로고    scopus 로고
    • Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy
    • Furuike, S., T. Ito, and M. Yamazaki. 2001. Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy. FEBS Lett. 498:72-75.
    • (2001) FEBS Lett , vol.498 , pp. 72-75
    • Furuike, S.1    Ito, T.2    Yamazaki, M.3
  • 46
    • 27744511675 scopus 로고    scopus 로고
    • Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature
    • Toraya, S., T. Nagao, K. Norisada, S. Tuzi, H. Saito, S. Izumi, and A. Naito. 2005. Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature. Biophys. J. 89:3214-3222.
    • (2005) Biophys. J , vol.89 , pp. 3214-3222
    • Toraya, S.1    Nagao, T.2    Norisada, K.3    Tuzi, S.4    Saito, H.5    Izumi, S.6    Naito, A.7
  • 47
    • 33846857534 scopus 로고    scopus 로고
    • Vesicle fission of giant unilamellar vesicles of liquid-ordered-phase membranes induced by amphiphiles with a single long chain hydrocarbon chain
    • Inaoka, Y., and M. Yamazaki. 2007. Vesicle fission of giant unilamellar vesicles of liquid-ordered-phase membranes induced by amphiphiles with a single long chain hydrocarbon chain. Langmuir. 23:720-728.
    • (2007) Langmuir , vol.23 , pp. 720-728
    • Inaoka, Y.1    Yamazaki, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.