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A new labdane diterpenoid, in vitro and in silico cytotoxicity, and protease inhibitory effects of phytochemicals from Juniperus polycarposK. Koch leaves.
Naderian, Moslem; Hafez Ghoran, Salar; Abdjan, Muhammad Ikhlas; Sabahi, Zahra; Moein, Soheila; Jassbi, Amir Reza; Moein, Mahmoodreza.
Afiliación
  • Naderian M; Department of Pharmacognosy, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Hafez Ghoran S; H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, Pakistan.
  • Abdjan MI; Phytochemistry Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
  • Sabahi Z; Department of Chemistry, Faculty of Science and Technology, Universitas Airlangga, Surabaya, Indonesia.
  • Moein S; Medicinal Plants Processing Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Jassbi AR; Medicinal Plants Processing Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Moein M; Medicinal and Natural Products Chemistry Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
Nat Prod Res ; : 1-12, 2024 Mar 19.
Article en En | MEDLINE | ID: mdl-38501578
ABSTRACT
Cytotoxicity-guided purification of Juniperus polycarpos K. Koch leaves (Cupressaceae) led to the isolation of a new labdane diterpenoid, 3-(acetyloxy)-acetylisocupressic acid (1), together with isocupressic acid (2), 3,4-dimethoxycinnamoyl alcohol (3) and deoxypodophyllotoxin (4). The chemical structures of 1-4 were established by detailed 1D and 2D NMR, HRFAB-MS and LRESI-MS, as well as by comparing the spectral data with those reported in the literature. Compound 1 was ineffective against HepG2 cells and protease enzyme, while 2 showed potent cytotoxicity against HepG2 cells (IC50 of 3.73 µg/mL) compared to cisplatin (IC50 of 12.65 µg/mL). Computational analyses with CDK1 protein (a prominent protein in the cell cycle of HepG2 cells) revealed the binding affinity of 2 (-31.86 kcal/mol) was better than 1 (-19.70 kcal/mol) because the acetoxy groups did not allow binding deeply to the ATP binding site. Compounds 2 and 4 moderately inhibited the protease activity (IC50 = 52.7 and 63.0 µg/mL, respectively). Further in vitro and in vivo studies on the plant are strongly recommended.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Nat Prod Res Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Nat Prod Res Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Reino Unido