Urease Inhibitory Activity of Aerial Parts of Artemisia scoparia: Exploration in an In Vitro Study

Artimisia scoparia has been used in the treatment of different disorders including ulcers. The current study was therefore designed to investigate the aerial parts of？？Artemisia scoparia (crude extract, total sterol and flavonoidal contents, and aqueous fraction) for its urease inhibitory potential. The crude of the plant evoked marked attenuation on urease activity, when tested in various concentrations with IC50 values of 4.06？mg/ml. The inhibitory potential was further augmented in the aqueous fraction (IC50: 2.30？mg/ml) of the plant. When the total sterol and flavonoidal contents were challenged against urease, both showed concentration dependent activity; the latter showed maximum potency with IC50 values of 8.04 and 2.10？mg/ml, respectively. In short, the aerial parts of the plant demonstrated marked antagonism on urease and thus our study validated the traditional use of Artemisia scoparia in the treatment of ulcer. 1. Introduction Urease (urea amidohydrolase) is usually found in different bacteria, fungi, algae, and plants, an enzyme that catalyzes the hydrolysis of urea to ammonia and carbamate, which is the final step of nitrogen metabolism in living organisms [1]. Carbamate rapidly and spontaneously decomposes, yielding a second molecule of ammonia. These reactions may cause significant increase in pH and are responsible for negative effects of urease activity in human health and agriculture [2, 3]. From the medical viewpoint, infections produced by these bacteria such as Helicobacter pylori and Proteus mirabilis usually have a high urease activity. Urease is central to H. pylori metabolism and virulence, is necessary for its colonization of the gastric mucosa, and is a potent immunogen that elicits a vigorous immune response. This enzyme is used for taxonomic identification and for diagnosis and followup after treatment and is a vaccine candidate. Urease represents an interesting model for metalloenzyme studies. Before the discovery of H. pylori, humans were thought to produce “gastric urease.” It is now known that the source of this notable protein is this bacterium, which colonizes the gastric mucosa of humans. It contributes in urinary tract and gastrointestinal infections, probably augmenting the severity of several pathological conditions like peptic ulcers and stomach cancer as in the case of H. pylori. Ureases are also involved in the development of different human and animal pathogenicity of urolithiasis, pyelonephritis, hepatic encephalopathy, hepatic coma, and urinary catheter encrustation [4–6]. Being involved in the