Naslov
Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase

Autori
Katalinić, Maja ; Rusak, Gordana ; Domaćinović Barović, Jelena ; Šinko, Goran ; Jelić, Dubravko ; Antolović, Roberto ; Kovarik, Zrinka

Izvornik
European journal of medicinal chemistry (0223-5234) 45 (2010), 1; 186-192

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
cholinesterase ; cytotoxicity ; flavonoids ; UV-VIS spectra ; reversible inhibition

Sažetak
Selected flavonoids: galangin, kaempferol, quercetin, myricetin, fisetin, apigenin, luteolin and rutin, reversibly inhibited human butyrylcholinesterase (BChE, EC 3.1.1.8). The enzymeinhibitor dissociation constants (Ki) ranged from 10 μ mol/L to 500 μ mol/L. Analysis of flavonoids chemical structure attributes their inhibition potency to the number of OH groups on their side phenyl ring. Docking study showed that flavonoids bind to the BChE active site by forming multiple hydrogen bonds and π -π interactions. The UV-VIS (200-500 nm) absorption spectra of flavonoids buffer solution, with the exception of rutin, revealed time dependant changes indicating precipitation of flavonoids or in the case of myricetin, change in the chemical structure resulting with BChE non-inhibiting specie. Quercetin and rutin, as two representative flavonoids, did not show cytotoxic effect on selected cell lines at concentrations up to 200 μ mol/L.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija, Farmacija

POVEZANOST RADA