Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase (CROSBI ID 153510)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Katalinić, Maja ; Rusak, Gordana ; Domaćinović Barović, Jelena ; Šinko, Goran ; Jelić, Dubravko ; Antolović, Roberto ; Kovarik, Zrinka
engleski
Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase
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.
cholinesterase ; cytotoxicity ; flavonoids ; UV-VIS spectra ; reversible inhibition
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Podaci o izdanju
45 (1)
2010.
186-192
objavljeno
0223-5234
10.1016/j.ejmech.2009.09.041
Povezanost rada
Kemija, Biologija, Farmacija