Assessing the ethnobotanical potential of Carissa opaca berries by merging outcomes from metabolomics profiling, enzyme assays, and in silico docking studies. (30th November 2021)

• Record Type: Journal Article
• Authors: Bashir, Kashif; Naz, Sadia; Farooq, Umar; Wahid, Fazli; Shah, Abdul Jabbar; McCauley, Erin P.; Crews, Phillip; Khan, Taous
• Is Part Of: Food chemistry. Volume 363(2021)
• Publication Date: 2021-11-30
• Subjects: Carissa opaca fruit -- α-Glucosidase inhibition -- LC–MS/MS-based molecular networking -- Molecular docking -- Polyphenolics -- Urease inhibition; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.130259
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: LC–MS/MS and molecular networking was used for chemical profiling of C. opaca fruit. A total of 25 compounds were observed in extract and fractions. Flavonoids, phenolics and triterpenoids were annotated as major classes of compounds. Extract and fractions inhibited activity of α-glucosidase and urease. Abstract: The phytochemical profile of Carissa opaca fruit extract and fractions was established through dereplication strategies employing LC-MS/MS and global natural product social molecular networking (GNPS). Crude extract and fractions were evaluated for their potential to inhibit α -glucosidase and urease in vitro . Flavonoid-O-glycosides, flavonoid-C-glycosides, flavonoids, proanthocyanidin B2, phenolics, and triterpenoids were annotated as the major classes of secondary metabolites present in the extract and fractions. α -Glucosidase inhibition was associated with n -butanol and ethyl acetate fractions comparable to acarbose (IC50 = 120.43 µg/mL) with IC50 values of 123.67 and 131.72 µg/mL, respectively. The ethyl acetate fraction showed good urease inhibition comparable with thiourea (IC50 = 103.71 µg/mL) with an IC50 value of 109.14 µg/mL. Molecular docking studies of compounds observed in the crude extract and bioactive fractions had significant binding scores, which supported results for enzyme inhibition in vitro . This study provided a detailed phytochemical profile of C. opaca fruit and its enzyme inhibition potential.