Pregled bibliografske jedinice broj: 717445
EVALUATION OF THE POTENCY OF A NEW SERIES OF PYRIDOXAL OXIME DERIVATIVES IN THE REACTIVATION OF TABUN, PARAOXON AND VX-PHOSPHYLATED ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE
EVALUATION OF THE POTENCY OF A NEW SERIES OF PYRIDOXAL OXIME DERIVATIVES IN THE REACTIVATION OF TABUN, PARAOXON AND VX-PHOSPHYLATED ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE // The Interply of Biomolecules HDBMB2014, Congress of the Croatian Society of Biochemistry and Molecular Biology, 24-27 September, 2014, Zadar, Croatia / Katalinić, Maja ; Kovarik, Zrinka (ur.).
Zadar: Hrvatsko Društvo za Biotehnologiju, 2014. str. 82-82 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 717445 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
EVALUATION OF THE POTENCY OF A NEW SERIES OF PYRIDOXAL OXIME DERIVATIVES IN THE REACTIVATION OF TABUN, PARAOXON AND VX-PHOSPHYLATED ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE
(EVALUATION OF THE POTENCY OF A NEW SERIES OF PYRIDOXAL OXIME DERIVATIVES IN THE REACTIVATION OF TABUN, PARAOXON AND VX-PHOSPHYLATED)
Autori
Bušić, Valentina ; Gašo-Sokač, Dajana ; Katalinić, Maja
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
The Interply of Biomolecules HDBMB2014, Congress of the Croatian Society of Biochemistry and Molecular Biology, 24-27 September, 2014, Zadar, Croatia
/ Katalinić, Maja ; Kovarik, Zrinka - Zadar : Hrvatsko Društvo za Biotehnologiju, 2014, 82-82
ISBN
978-953-95551-5-1
Skup
Congress of the Croatian Society of Biochemistry and Molecular Biology
Mjesto i datum
Zadar, Hrvatska, 24.09.2014. - 27.09.2014
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
acetylcholinesterase; butyrylcholinesterase; pyridoxal oxime; reactivation of phosphylated enzymes; reversible inhibition
Sažetak
Quaternary salts of pyridoxal oxime were synthesized by the quaternization of the pyridoxal oxime with substituted phenacyl bromides using microwave heating. Microwave-assisted rapid synthesis was done in solvent (acetone) and under solvent-free condition. In this study we investigated these new oxime interactions with human recombinant acetylcholinesterase (AChE, EC 3.1.1.7) and human butyrylcholinesterase (BChE, EC 3.1.1.8). We tested the oxime’s reversible inhibition of enzymes and oxime-assisted reactivation of phosphylated enzymes. All of the tested oximes reversibly inhibited AChE and BChE with inhibition constants (Ki) in micromolar to milimolar range but showing week enzyme selectivity. Furthermore, the oximes were tested in 1 mM concentration as reactivators of AChE and BChE inhibited by organophosphorus compounds tabun, paraoxon and VX. Unfortunately, the tested oximes were not efficient in reactivation of either tabun, paraoxon or VX inhibited enzymes, especially compared to the oximes currently used in medical treatment practice. However two of tested oximes showed a potency to reactivate BChE inhibited by VX, and therefore could be considered in the area of organophosphorus compounds bioscavenger development and pre-treatment drugs.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb,
Prehrambeno-tehnološki fakultet, Osijek
