Article Publish Status: FREE
Abstract Title:

Zerumbone InhibitsUrease Activity.

Abstract Source:

Molecules. 2021 May 1 ;26(9). Epub 2021 May 1. PMID: 34062878

Abstract Author(s):

Hyun Jun Woo, Ji Yeong Yang, Pyeongjae Lee, Jong-Bae Kim, Sa-Hyun Kim

Article Affiliation:

Hyun Jun Woo


() produces urease in order to improve its settlement and growth in the human gastric epithelium. Urease inhibitors likely represent potentially powerful therapeutics for treating; however, their instability and toxicity have proven problematic in human clinical trials. In this study, we investigate the ability of a natural compound extracted fromSmith, zerumbone, to inhibit the urease activity ofby formation of urease dimers, trimers, or tetramers. As an oxygen atom possesses stronger electronegativity than the first carbon atom bonded to it, in the zerumbone structure, the neighboring second carbon atom shows a relatively negative charge (δ) and the next carbon atom shows a positive charge (δ), sequentially. Due to this electrical gradient, it is possible thaturease with its negative charges (such as thiol radicals) might bind to theβ-position carbon of zerumbone. Our results show that zerumbone dimerized, trimerized, or tetramerized with bothurease A and urease B molecules, and that this formation of complex inhibitedurease activity. Although zerumbone did not affect either gene transcription or the protein expression of urease A and urease B, our study demonstrated that zerumbone could effectively dimerize with both urease molecules and caused significant functional inhibition of urease activity. In short, our findings suggest that zerumbone may be an effectiveurease inhibitor that may be suitable for therapeutic use in humans.

Study Type : In Vitro Study

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