Naslov
Cholinesterase interactions with oximes

Autori
Kovarik, Zrinka ; Katalinić, Maja ; Bosak, Anita ; Šinko, Goran

Izvornik
Current bioactive compounds (1573-4072) 6 (2010), 1; 9-15

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, pregledni rad, znanstveni

Ključne riječi
Acetylcholinesterase; Antidote; Bioscavenger; Butyrylcholinesterase; Nerve agents; Tabun; Oxime; Treatment

Sažetak
The phosphorylation of the serine hydroxyl group in the active site of acetylcholinesterase (AChE) inactivates this essential enzyme in neurotransmission. Oximes are reactivators of AChE phosphorylated by organophosphorus compounds (OP) including insecticides and nerve agents. The effectiveness of oxime-assisted reactivation is primarily attributed to the nucleophilic displacement rate of organophosphate, but efficiency varies with the structure of the bound organophosphate, the structure of the oxime as well as rates of several other cholinesterase's reactions. Besides reactivating cholinesterases, oximes also reversibly inhibit cholinesterases and protect them from phosphorylation by OP. In this paper, we bring an overview of in vitro native and tabun-inhibited AChE and butyrylcholinesterase interactions with oximes together with conformational analysis of the oximes to relate molecular properties to their reactivation potency.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA