6533b871fe1ef96bd12d1b6a

RESEARCH PRODUCT

Metabolite profile and in vitro activities of Phagnalon saxatile (L.) Cass. relevant to treatment of Alzheimer’s disease

Maurizio BrunoFilomena ConfortiFelice SenatoreMonica R. LoizzoFrancesco MenichiniDaniela RiganoCarmen Formisano

subject

AntioxidantDPPHmedicine.medical_treatmentMetaboliteAsteraceaePharmacologyNitric OxideInhibition of NO productionCell LineMicechemistry.chemical_compoundPhagnalon saxatileAlzheimer DiseaseDrug DiscoverymedicineCaffeic acidAnimalsHumansSettore BIO/15 - Biologia FarmaceuticaIC50ButyrylcholinesterasePharmacologyPlant Extractsinhibition of NO production Alzheimer's diseaseSettore CHIM/06 - Chimica OrganicaGeneral MedicineAcetylcholinesterasePhenolic compoundsAlzheimers diseasechemistryBiochemistryPhagnalon saxatile asteraceae phenolic compoundButyrylcholinesteraseAcetylcholinesteraseCholinesterase InhibitorsLuteolin

description

The present study describes for the first time the in vitro properties (inhibition of NO production and anticholinesterase) of Phagnalon saxatile (L.) Cass. (Asteraceae). The methanolic extract showed antioxidant activity that was measured by DPPH assay and beta-carotene bleaching test. The same extract inhibited NO production in the murine monocytic macrophage cell line RAW 264.7. Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibition was assessed by modifications of Ellman's method. Purification of the MeOH extract of P. saxatile allowed the isolation of phenolic compounds. Among them, the compounds that most effectively inhibited lipopolysaccharide-induced NO production were caffeic acid and methylchlorogenic acid, with IC50 values of 7 microg/mL and 12 microg/mL, respectively. Luteolin and 3,5-dicaffeoylquinic acid exhibited the most promising activity against AChE with an IC50 of 25.2 and 54.5 microg/mL, respectively, while caffeic acid and luteolin exhibited higher activity against BChE with an IC50 of 32.2 and 37.2 microg/mL, respectively.

yearjournalcountryeditionlanguage
2009-12-25Journal of Enzyme Inhibition and Medicinal Chemistry
https://doi.org/10.3109/14756360903018260