Photodynamic cytotoxic effect of Marrubium parviflorum and molecular docking–based network target identification of its major phytocompounds


AYTAR E. C., ÇALIŞKAN M., Caliskan S., Gümrükçüoğlu A., Torunoğlu E. İ., Doğu S.

Plant Biosystems, cilt.160, sa.2, 2026 (SCI-Expanded, Scopus) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 160 Sayı: 2
  • Basım Tarihi: 2026
  • Doi Numarası: 10.1007/s44473-026-00105-9
  • Dergi Adı: Plant Biosystems
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Environment Index
  • Anahtar Kelimeler: Marrubium parviflorum, Molecular docking, Photodynamic therapy, Protein–protein interaction
  • Uşak Üniversitesi Adresli: Evet

Özet

The use of plants in drug discovery has gained increasing importance due to their diverse pharmacological activities. This study aimed to investigate the phytochemical composition, molecular targets, and anticancer potential of Marrubium parviflorum subsp. parviflorum. The extract was analyzed for its chemical composition, followed by protein target prediction, PPI network analysis, and molecular docking studies. Cytotoxicity was evaluated in lung (A549), breast (MCF-7), colorectal (HT-29), and normal kidney (HEK293) cell lines under different light conditions. HEK293 cells, a non-tumour human kidney cell line, were included as a normal control to evaluate whether the extract exerted selective anticancer effects under both dark and light conditions. Twenty compounds were identified, with α-pinene, d-limonene, rutin, and quercetin as major constituents. Rutin and quercetin showed strong binding affinities with AKT1 and MMP9 proteins. The extract alone exhibited no significant anticancer activity. However, under photodynamic therapy with yellow light, cytotoxicity was markedly enhanced, showing the lowest IC₅₀ values (HEK293: 402 µg/mL; HT-29: 516 µg/mL). These findings suggest that while M. parviflorum extract lacks standalone anticancer effects, its activity increases under light exposure, likely mediated by rutin and quercetin through AKT1 and MMP9 inhibition.