Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cells
Autor: | Emi Hibino, Natsuko Goda, Misaki Hisada, Takeshi Tenno, Hidekazu Hiroaki |
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Rok vydání: | 2022 |
Předmět: | |
Zdroj: | Food & Function. 13:1953-1964 |
ISSN: | 2042-650X 2042-6496 |
Popis: | Glycyrrhizin (GL) is known to exhibit a variety of useful pharmacological activities, including anti-inflammation, anti-hepatotoxicity, and enhancement of intestinal drug absorption. GL has been reported to modify the assembly of actin filaments, thereby modulating tight junction (TJ) integrity, but the detailed molecular mechanisms of this remain unclear. In this study, we first found that GL binds to the first PDZ domain of zonula occludens-1 (ZO-1(PDZ1)) through NMR experiments. The structure of the GL-ZO-1(PDZ1) complex was then constructed using HADDOCK with the transferred nuclear Overhauser effect-based inter-hydrogen distance constraints as well as restrictions on the interfacial residues identified from |
Databáze: | OpenAIRE |
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