Mechanism of protein tyrosine phosphatase 1B inhibition by theaflavanoside IV isolated from methanolic extract of tea (Camellia sinensis) seed shells
- Authors
- Woo, Hyun Sim; Im, Hyeon Jeong; Kim, Jeong Yoon; Lee, Min-Sung; Kim, Dae Wook
- Issue Date
- 15-Jun-2022
- Publisher
- TAYLOR & FRANCIS LTD
- Keywords
- Camellia sinensis seed shell; theaflavanoside IV; caffeine; protein tyrosine phosphatase 1B; competitive inhibition; slow binding
- Citation
- NATURAL PRODUCT RESEARCH, v.36, no.12, pp.3189 - 3192
- Indexed
- SCIE
SCOPUS
- Journal Title
- NATURAL PRODUCT RESEARCH
- Volume
- 36
- Number
- 12
- Start Page
- 3189
- End Page
- 3192
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/1163
- DOI
- 10.1080/14786419.2021.1952576
- ISSN
- 1478-6419
- Abstract
- Camellia sinensis (tea) seeds have been identified as potential sources of nutraceutical compounds. In this study, caffeine and theaflavanoside IV were annotated as the most abundant phytochemicals in the seed shells of C. sinensis. Both compound displayed potent inhibitions against protein tyrosine phosphatase 1B (PTP1B) with IC50 values of 37.9 +/- 3.5 and 8.7 +/- 1.1 mu M, respectively. In the kinetic study, caffeine inhibited PTP1B with mixed type I mode, which prefers to bind to free enzyme. Theaflavanoside IV showed competitive and reversible simple slow-binding inhibition [k(3) = 0.1 mu M-1 center dot min(-1), k(4) = 0.002 min(-1), K-i(app) = 0.0002 mu M]. This is the first report on PTP1B-inhibitory activity of these compounds and their action mechanisms. These results suggest their potential in the development of antidiabetic agents.
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