English  |  正體中文  |  简体中文  |  Items with full text/Total items : 66984/66984 (100%)
Visitors : 23029932      Online Users : 392
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version


    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/38945


    Title: Interaction of Tea Catechin (-)-Epigallocatechin Gallate with Lipid Bilayers
    Authors: Sun,Y;Hung,WC;Chen,FY;Lee,CC;Huang,HW
    Contributors: 物理研究所
    Keywords: ANTIMICROBIAL PEPTIDES;PORE FORMATION;DIPHYTANOYL PHOSPHATIDYLCHOLINE;SPONTANEOUS-CURVATURE;GREEN TEA;MEMBRANE;VESICLES;MODEL;MECHANISM;CURCUMIN
    Date: 2009
    Issue Date: 2010-07-08 13:59:59 (UTC+8)
    Publisher: 中央大學
    Abstract: A major component of green tea extracts, catechin(-)-Epigallocatechin gal late (EGCg), has been reported to be biologically active and interacting with membranes. A recent study reported drastic effects of EGCg on giant unilamellar vesicles (GUVs). In particular, EGCg above 30 mu M caused GUVs to burst. Here we investigated the effect of EGCg on single GUVs at lower concentrations, believing that its molecular mechanism would be more clearly revealed. We used the micropipette aspiration method, by which the changes of surface area and volume of a GUV could be measured as a result of interaction with EGCg. We also used x-ray diffraction to measure the membrane thinning effect by EGCg. To understand the property of EGCg, we compared its effect with other membrane-active molecules, including pore-forming peptide magainin, the turmeric (curry) extract curcumin, and detergent Triton X100. We found the effect of EGCg somewhat unique. Although EGCg readily binds to lipid bilayers, its membrane area expansion effect is one order of magnitude smaller than curcumin. EGCg also solubilizes lipid molecules from lipid bilayers without forming pores, but its effect is different from that of Triton X100.
    Relation: BIOPHYSICAL JOURNAL
    Appears in Collections:[物理研究所] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML528View/Open


    All items in NCUIR are protected by copyright, with all rights reserved.

    社群 sharing

    ::: Copyright National Central University. | 國立中央大學圖書館版權所有 | 收藏本站 | 設為首頁 | 最佳瀏覽畫面: 1024*768 | 建站日期:8-24-2009 :::
    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback  - 隱私權政策聲明