Rubusuaviins A-F, Monomeric and Oligomeric Ellagitannins from Chinese Sweet Tea and Their α-Amylase Inhibitory Activity Rubusuaviins A-F, Monomeric and Oligomeric Ellagitannins from Chinese Sweet Tea and Their α-Amylase Inhibitory Activity

    • LI Haizhou
    • Graduate School of Biomedical Sciences, Nagasaki University
    • ZHANG Ying-Jun
    • Laboratory of Phytochemistry, Kunming Institute of Botany, Chinese Academy of Sciences
    • YANG Chong-Ren
    • Laboratory of Phytochemistry, Kunming Institute of Botany, Chinese Academy of Sciences

    • KOUNO Isao
    • Graduate School of Biomedical Sciences, Nagasaki University

Abstract

Six new ellagitannins herein, rubusuaviins A?F, were isolated from the aqueous acetone extract of Chinese sweet tea (Tien-cha, dried leaves of Rubus suavissimus S. LEE) together with seven known tannins. Rubusuaviin A was characterized as 1-O-galloyl-2,3-O-(S)-HHDP-4,6-O-(S)-sanguisorboyl-β-D-glucopyranose. Rubusuaviins B, C, and E are dimeric, trimeric, and tetrameric ellagitannins, respectively, in which the sanguisorboyl groups were connected ellagitannin units. Rubusuaviins D and F were desgalloyl derivatives of rubusuaviins C and E, respectively. The inhibition of α-amylase activity by rubusuaviins and related ellagitannins was compared. Ellagitannins with β-galloyl groups at the glucose C-1 positions showed stronger inhibition compared with the α-galloyl and desgalloyl compounds. The molecular weight of these compounds was not important for the inhibition of α-amylase activity.

Six new ellagitannins herein, rubusuaviins A-F, were isolated from the aqueous acetone extract of Chinese sweet tea (Tien-cha, dried leaves of Rubus suavissimus S. LEE) together with seven known tannins. Rubusuaviin A was characterized as 1-O-galloyl-2,3-O-(S)-HHDP-4,6-O-(S)-sanguisorboyl-β-D-glucopyranose. Rubusuaviins B, C, and E are dimeric, trimeric, and tetrameric ellagitannins, respectively, in which the sanguisorboyl groups were connected ellagitannin units. Rubusuaviins D and F were desgalloyl derivatives of rubusuaviins C and E, respectively. The inhibition of α-amylase activity by rubusuaviins and related ellagitannins was compared. Ellagitannins with β-galloyl groups at the glucose C-1 positions showed stronger inhibition compared with the α-galloyl and desgalloyl compounds. The molecular weight of these compounds was not important for the inhibition of α-amylase activity.

Journal

Chemical & pharmaceutical bulletin   [List of Volumes]

Chemical & pharmaceutical bulletin 55(9), 1325-1331, 2007-09-01  [Table of Contents]

The Pharmaceutical Society of Japan

References:  18

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Codes

  • NII Article ID (NAID) :
    110006379652
  • NII NACSIS-CAT ID (NCID) :
    AA00602100
  • Text Lang :
    ENG
  • Article Type :
    Journal Article
  • ISSN :
    00092363
  • NDL Article ID :
    8877606
  • NDL Source Classification :
    ZS51(科学技術--薬学) // ZP1(科学技術--化学・化学工業)
  • NDL Call No. :
    Z53-D167
  • Databases :
    CJP  CJPref  NDL  NII-ELS  IR  J-STAGE 

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