Naslov
Interaction of flavonoids with butyrylcholinesterase

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

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
The FEBS Journal, Vol. 276, Supplement 1. 34th FEBS Congress: "Life´s Molecular Interactions" / - Oxford : Wiley-Blackwell, 2009, 320-321

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

Mjesto i datum
Prag, Češka Republika, 04.07.2009. - 09.07.2009

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Flavonoids; Cholinesterase; Reversible Inhibition; Alzheimer Disease
(flavonoids; cholinesterase; reversible inhibition; alzheimer disease)

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

Napomena
DOI: 10.1111/j.1742-4658.2009.07049.x

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