Prolyl endopeptidase-lnhibiting antioxidant fromPhyllanthus ussurensis

A prolyl endopeptidase inhibitor was isolated from the ethyl acetate soluble fraction ofPhyllanthus ussurensis. The active compound was identified as an ellagitannin, corilagin. It was shown to non-competitively inhibit prolyl endopeptidase (PEP) with the IC₅₀ value of 1.17x10⁻⁶ μM. TheKi value was...

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Published inArchives of pharmacal research Vol. 26; no. 12; pp. 1024 - 1028
Main Authors Chung, Shin-Kyo, Nam, Ji-Ae, Jeon, So-Young, Kim, Sang-In, Lee, Hee-Ju, Chung, Tai Ho, Song, Kyung-Sik
Format Journal Article
LanguageEnglish
Published Pharmaceutical Society of Korea 01.12.2003
Subjects
anions
antioxidants
chymotrypsin
elastase
ethyl acetate
hydrogen peroxide
inhibitory concentration 50
reactive oxygen species
superoxide anion
trypsin
xanthine oxidase
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Summary:A prolyl endopeptidase inhibitor was isolated from the ethyl acetate soluble fraction ofPhyllanthus ussurensis. The active compound was identified as an ellagitannin, corilagin. It was shown to non-competitively inhibit prolyl endopeptidase (PEP) with the IC₅₀ value of 1.17x10⁻⁶ μM. TheKi value was 6.70x10⁻⁷ M. Corilagin was less inhibitory to other serine proteases such as chymotrypsin, trypsin, and elastase, indicating that it was relatively a specific inhibitor of PEP. Corilagin also effectively inhibited reactive oxygen species such as hydroxide and superoxide anion radical, hydrogen peroxide, and DPPH. Especially, corilagin showed potent scavenging activity on the superoxide anion radical in the ESR method (IC₅₀ = 3.79x10⁻⁶ M) as well as xanthine oxidase system.
Bibliography:http://dx.doi.org/10.1007/BF02994753
ISSN:0253-6269
1976-3786
DOI:10.1007/BF02994753