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izvor podataka: crosbi

Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase (CROSBI ID 153510)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Katalinić, Maja ; Rusak, Gordana ; Domaćinović Barović, Jelena ; Šinko, Goran ; Jelić, Dubravko ; Antolović, Roberto ; Kovarik, Zrinka Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase // European journal of medicinal chemistry, 45 (2010), 1; 186-192. doi: 10.1016/j.ejmech.2009.09.041

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

Poveznice
Indeksiranost