Targeted Phenolic Profiling, Antioxidant Activities, and Enzyme Inhibition Potential of Campanula lyrata subsp. lyrata Extracts With Molecular Docking Insights

Solmaz F. O. K., Kirkan B., İstifli E. S., Sarikurkcu C., Tepe B.

JOURNAL OF FOOD SCIENCE, cilt.90, ss.1-21, 2025 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 90
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1111/1750-3841.70368
  • Dergi Adı: JOURNAL OF FOOD SCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Agricultural & Environmental Science Database, Analytical Abstracts, Applied Science & Technology Source, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Computer & Applied Sciences, Environment Index, Food Science & Technology Abstracts, INSPEC, Veterinary Science Database, DIALNET
  • Sayfa Sayıları: ss.1-21
  • Çukurova Üniversitesi Adresli: Evet

Özet

The growing interest in plant-based bioactives has intensified research into their therapeutic potential. This studyinvestigated the chemical profile, antioxidant properties, and enzyme inhibitory effects of methanol extracts from Campanulalyrata subsp. lyrata, obtained via maceration (MAC-ME), Soxhlet (SOE-ME), and ultrasound-assisted extraction (UAE-ME).Among the extracts, MAC-ME contained the highest total phenolic (41.76 mg GAE/g) and flavonoid (23.68 mg RE/g) contents.In antioxidant assays, SOE-ME exhibited the strongest DPPH radical scavenging activity (IC50 : 1.17 mg/mL), while all extractsdisplayed comparable reducing power in CUPRAC and FRAP assays (EC50 : 0.50–0.77 mg/mL), indicating moderate antioxidantpotential. Enzyme inhibition results revealed that SOE-ME showed the most potent AChE (IC50 : 1.18 ± 0.03 mg/mL) and tyrosinase(IC50 : 1.45 ± 0.01 mg/mL) inhibition, whereas MAC-ME demonstrated the highest α-amylase inhibition (IC50 : 2.11 ± 0.01 mg/mL).These findings suggest selective bioactivity profiles depending on the extraction technique. Molecular docking supported thein vitro results, showing strong binding affinities of chlorogenic acid (ΔG = −9.25 kcal/mol for AChE) and hesperidin (ΔG =−9.05 kcal/mol for α-amylase), with simultaneous docking indicating potential synergistic interactions (ΔG up to −12.65 kcal/mol).Overall, the extracts—especially SOE-ME—demonstrated promising multi-target bioactivity, underscoring the pharmacologicalpotential of C. lyrata subsp. lyrata in managing oxidative stress and enzyme-related disorders..