Naslov
Interaction of pyridinium oximes K027, K033 and K048 with native and tabun-inhibited human acetylcholinesterase

Autori
Kovarik, Zrinka ; Čalić, Maja ; Kuča Kamil ; Jun, Daniel

Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni

Izvornik
The Proceedings of the Chemical and Biological Medical Treatment Symposium CB MTS - Industry IV "The Third World Congress on Chemical, Biological and Radiological Terrorism" / Bokan, Slavko ; Orehovec, Zvonko ; Price, Barbara - Aberdeen (MD) : Applied Science and Analysis, 2006, 173-175

Skup
CB MTS-Industry IV "The Third World Congress on Chemical, Biological and Radiological Terrorism"

Mjesto i datum
Dubrovnik, Hrvatska, 17.09.2005. - 23.09.2005

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Acetylcholinesterase; Antidotes; Inhibition; Protection; Reactivation; Warfare nerve agents

Sažetak
This study examined the ability of three bispyridinium oximes K027 [1-(4-hydroxyiminomethylpyridinium)-3-(4-carbamoylpyridinium) propane dibromide], K048 [1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium) butane dibromide], and K033 [1, 4-bis(2-hydroxyiminomethylpyridinium) butane dibromide] to reactivate tabun-inhibited human erythrocyte AChE. Reversible inhibition of native AChE by these oximes and their protective index of AChE inactivation by tabun were determined as well. Tabun-inhibited AChE was completely reactivated by micromolar concentrations of K027 and K048. The reactivation by K033 reached 50 % after 24 hours. All the oximes were reversible inhibitors of AChE, and dissociation constants were 17 μ M, 73 μ M and 110 μ M for K033, K027 and K048, respectively. All studied oximes protected the enzyme from phosphonylation by tabun by at least factor 2. Our in vitro experiments pointed out K048 and K027 as promising reactivators, while K033 showed promise as a protective agent in tabun poisoning.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA