Naslov
Evaluation of flavonoids potency to inhibit human butyrylcholinesterase

Autori
Čalić, Maja ; Domaćinović, Jelena ; Rusak, Gordana ; Kovarik, Zrinka

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

Izvornik
Congress of the Croatian Society of the Biochemistry and Molecular Biology on the occasion of the 30th Anniversary with international participation, Book of Abstracts / Kovarik, Zrinka - Zagreb : Hrvatsko društvo za biokemiju i molekularnu biologiju (HDBMB), 2006

Skup
Congress of the Croatian Society of the Biochemistry and Molecular Biology on the occasion of the 30th Anniversary with international participation

Mjesto i datum
Vodice, Hrvatska, 03.10.2006. - 07.10.2006

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
flavonoids; butyrylcholinesterase; inhibition

Sažetak
Butyrylcholinesterase (BChE ; 3.1.1.8) is a serine hydrolase that belongs to the lipase/protease family with &#945; /&#946; -hydrolase fold. Opposite to the key role in cholinergic neurotransmission of its sister enzyme, acetylcholinesterase (AChE ; 3.1.1.7), the real physiological function of BChE is yet unknown. However, it has been shown that BChE can also hydrolyse the native substrate of AChE, neurotransmitter acetylcholine, and thus serve as a co-regulator of cholinergic transmission. This is why the inhibition of BChE, not only of AChE, 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 and luteolin ; 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.). Inhibition potency was determined on BChE containing native human plasma samples. Results of our experiments showed that all tested flavonoids reversibly inhibited BChE and the evaluated enzyme-inhibitor dissociation constants (Ki) ranged from 10 &#956; M to 140 &#956; M. The inhibition potency increased in the following order: luteolin<fisetin<myricetin<quercetin<kaempferol<apigenin<galangin. With the lowest observed Ki value of 10 &#956; M, galangin was pointed out as a promising lead in the search for new BChE inhibitors.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA