Akademik Veri Yönetim Sistemi
Chemistry and Biodiversity, 2025 (SCI-Expanded, Scopus)
An ever-increasing number of ailments are being treated using Hypericum L. species, which are gaining both popular and scientific relevance. This study set out to thoroughly examine the chemical and biological aspects of ethanol extracts from the roots and aerial parts of the Hypericum empetrifolium subsp. empetrifolium Willd., Hypericum triquetrifolium Turra, and Hypericum pruinatum Boiss. Et. Honey species. Thus, it is aimed to shed light on the uses of Hypericum species among the public by revealing both their chemical and biological profiles. Species-specific phenolic content of the samples was determined by LC–MS/MS. In addition, antioxidant, anticholinesterase, urease, tyrosinase, elastase, collagenase, and angiotensin I-converting enzyme (ACE) inhibition activities of the extracts and some major components (chlorogenic acid, hesperidin, hyperoside, quercitrin, quercetin, pseudohypericin, hypericin) specific to Hypericum species were determined. LC–MS/MS results showed that some samples were rich in hyperoside (49 365.6 µg analyte/g extract), hesperidin (10 077.8), chlorogenic acid (15 027.8), luteolin-7-glycoside (1629.6), quercitrin (6979.7), pseudohypericin (998.8), and hypericin (386.5). The samples were found to have a high potential in CUPRAC, DPPH, and ABTS antioxidant methods. High enzyme activity was seen in particular for acetylcholinesterase (AChE) (inhibition%: 54.00 ± 0.97) H. pruinatum root ethanol extract, for butyrylcholinesterase (BChE) (inhibition%: 73.33 ± 1.49) of H. triquetrifolium aerial part ethanol extract, for urease (inhibition%: 49.20 ± 1.27) of H. empetrifolium subsp. empetrifolium aerial part ethanol extract, for tyrosinase (inhibition%: 55.40 ± 0.52) of H. pruinatum root ethanol extract, and elastase (inhibition%: 36.84 ± 0.45) of H. pruinatum aerial part ethanol extract. The enzyme inhibitory potentials of hesperidin (urease inhibition%: 54.32 ± 1.35, tyrosinase: 73.87 ± 2.06, elastase: 82.23 ± 1.41, collagenase: 67.37 ± 0.73, and ACE: 80.74 ± 0.85) and quercetin (AChE inhibition%: 57.82 ± 1.21, BChE: 92.82 ± 1.84, urease: 73.17 ± 1.79, tyrosinase: 65.25 ± 1.73, elastase: 98.04 ± 2.28, and ACE: 86.74 ± 0.85), principal constituents of Hypericum species, were shown to be significantly high on the basis of both in vitro and in silico analyses. The in vitro and in silico test findings of Hypericum species and their principal components indicate that they are promising sources of natural agents, suggesting their potential application in the food and pharmaceutical industries.