Urease Inhibitory Kinetic Studies of Various Extracts and Pure Compounds from Cinnamomum Genus

Molecules. 2021 Jun 22;26(13):3803. doi: 10.3390/molecules26133803.

Abstract

Urease is an enzyme that plays a significant role in the hydrolysis of urea into carbonic acid and ammonia via the carbamic acid formation. The resultant increase in pH leads to the onset of various pathologies such as gastric cancer, urolithiasis, hepatic coma, hepatic encephalopathy, duodenal ulcers and peptic ulcers. Urease inhibitors can reduce the urea hydrolysis rate and development of various diseases. The Cinnamomum genus is used in a large number of traditional medicines. It is well established that stem bark of Cinnamomum cassia exhibits antiulcerogenic potential. The present study evaluated the inhibitory effect of seven extracts of Cinnamomum camphora, Cinnamomum verum and two pure compounds Camphene and Cuminaldehyde on urease enzyme. Kinetic studies of potential inhibitors were carried out. Methanol extract (IC50 980 µg/mL) of C. camphora and a monoterpene Camphene (IC50 0.147 µg/mL) possess significant inhibitory activity. The Lineweaver Burk plot analysis suggested the competitive inhibition by methanol extract, hexane fraction and Camphene. The Gas Chromatography-Mass Spectroscopy (GC-MS) analysis of hexane fraction revealed the contribution of various terpenes. The present study targets terpenes as a new class of inhibitors that have potential therapeutic value for further development as novel drugs.

Keywords: Cinnamomum; camphene; cuminaldehyde; urease inhibition.

MeSH terms

  • Bacterial Proteins* / antagonists & inhibitors
  • Bacterial Proteins* / chemistry
  • Cinnamomum / chemistry*
  • Enzyme Inhibitors / chemistry*
  • Molecular Docking Simulation*
  • Plant Extracts / chemistry*
  • Urease* / antagonists & inhibitors
  • Urease* / chemistry

Substances

  • Bacterial Proteins
  • Enzyme Inhibitors
  • Plant Extracts
  • Urease