Inhibitory Activity of 4-O-Benzoyl-3′-O-(OMethylsinapoyl) Sucrose from Polygala tenuifolia on Escherichia coli β-Glucuronidase | Zendy

Jang Hoon Kim | Zendy; Le Ba Vinh | Zendy; Mok Hur | Zendy; Sung-Cheol Koo | Zendy; Woo Tae Park | Zendy; Youn-Ho Moon | Zendy; Yoon Jeong Lee | Zendy; Young Ho Kim | Zendy; Yun-Chan Huh | Zendy; Seo Young Yang | Zendy

Open Access

Inhibitory Activity of 4-O-Benzoyl-3′-O-(OMethylsinapoyl) Sucrose from Polygala tenuifolia on Escherichia coli β-Glucuronidase

Author(s) -

Jang Hoon Kim,

Le Ba Vinh,

Mok Hur,

Sung-Cheol Koo,

Woo Tae Park,

Youn-Ho Moon,

Yoon Jeong Lee,

Young Ho Kim,

Yun-Chan Huh,

Seo Young Yang

Publication year - 2021

Publication title -

journal of microbiology and biotechnology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.601

H-Index - 64

eISSN - 1738-8872

pISSN - 1017-7825

DOI - 10.4014/jmb.2108.08004

Subject(s) - escherichia coli , chemistry , sucrose , microbiology and biotechnology , biochemistry , stereochemistry , biology , gene

Bacterial β -glucuronidase in the intestine is involved in the conversion of 7-ethyl-10- hydroxycamptochecin glucuronide (derived from irinotecan) to 7-ethyl-10-hydroxycamptothecin, which causes intestinal bleeding and diarrhea (side effects of anti-cancer drugs). Twelve compounds (1-12) from Polygala tenuifolia were evaluated in terms of β -glucuronidase inhibition in vitro. 4- O -Benzoyl-3'-O-(O-methylsinapoyl) sucrose (C3) was highly inhibitory at low concentrations. C3 (an uncompetitive inhibitor) exhibited a k i value of 13.4 μM; inhibitory activity increased as the substrate concentration rose. Molecular simulation revealed that C3 bound principally to the Gln158-Tyr160 enzyme loop. Thus, C3 will serve as a lead compound for development of new β - glucuronidase inhibitors.

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