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Interaction of flavonoids with butyrylcholinesterase (CROSBI ID 557240)

Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija

Kovarik, Zrinka ; Šinko, Goran ; Katalinić, Maja ; Rusak, Gordana Interaction of flavonoids with butyrylcholinesterase // The FEBS journal. 2009. str. 320-321

Podaci o odgovornosti

Kovarik, Zrinka ; Šinko, Goran ; Katalinić, Maja ; Rusak, Gordana

engleski

Interaction of flavonoids with butyrylcholinesterase

Butyrylcholinesterase (BChE ; 3.1.1.8) is a serine hydrolase that belongs to the lipase/protease family with α/β-hydrolase fold. Although its exact physiological function remains unclear, it is known that BChE is responsible for the metabolism of various drugs. It can serve as a co-regulator of cholinergic neurotransmission and at high concentration BChE can efficently hydrolise neurotransmitter acetylcholine. This is why the inhibition of BChE appears to be of an interest in treating diseases having symptoms of reduced acetylcholine levels, such as the Alzheimer disease. We evaluated the BChE inhibition by seven selected flavonoids: galangin, kaempferol, quercetin, myricetin, fisetin, apigenin, luteolin and rutin ; belonging to a large family of biologically active polyphenolic compounds found in many plants and plant-derived products that are components of everyday human diet (fruits, vegetables, chocolates, herbs, red wine, tea, beer, etc.). All tested flavonoids reversibly inhibited BChE and the evaluated enzyme-inhibitor dissociation constants (Ki) ranged from 10 μM to 500 μM. The inhibition potency increased in the following order: rutin < luteolin < fisetin < myricetin < quercetin < kaempferol < apigenin < galangin. Docking study showed that flavonoids bind to the BChE active site by forming multiple hydrogen bonds and π- π interactions. With the lowest observed Ki value of 10 μM, galangin was pointed out as a promising lead in the search for new BChE inhibitors.

flavonoids; cholinesterase; reversible inhibition; alzheimer disease

DOI: 10.1111/j.1742-4658.2009.07049.x

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Podaci o prilogu

320-321.

2009.

nije evidentirano

objavljeno

Podaci o matičnoj publikaciji

The FEBS journal

Oxford: Wiley-Blackwell

1742-464X

Podaci o skupu

34th FEBS Congress: "Life´s Molecular Interactions"

poster

04.07.2009-09.07.2009

Prag, Češka Republika

Povezanost rada

Kemija, Biologija

Indeksiranost