Kuca_2009_Molecules_14_4915

Reference

Title : Novel bisquaternary oximes--reactivation of acetylcholinesterase and butyrylcholinesterase inhibited by paraoxon - Kuca_2009_Molecules_14_4915
Author(s) : Kuca K , Musilova L , Palecek J , Cirkva V , Paar M , Musilek K , Hrabinova M , Pohanka M , Karasova JZ , Jun D
Ref : Molecules , 14 :4915 , 2009
Abstract :

Four novel bisquaternary aldoxime cholinesterase reactivators differing in their chemical structure were prepared. Afterwards, their biological activity was evaluated for their ability to reactivate acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BuChE; EC 3.1.1.8) inhibited by paraoxon. Their reactivation activity was compared with standard reactivators--pralidoxime, obidoxime and HI-6--which are clinically used at present. As it resulted, none of the prepared compounds surpassed obidoxime, which is considered to be the most potent compound if used for reactivation of AChE inhibited by paraoxon. In case of BuChE reactivation, two compounds (K053 and K068) achieved similar results as obidoxime.

PubMedSearch : Kuca_2009_Molecules_14_4915
PubMedID: 20032868

Related information

Citations formats

Kuca K, Musilova L, Palecek J, Cirkva V, Paar M, Musilek K, Hrabinova M, Pohanka M, Karasova JZ, Jun D (2009)
Novel bisquaternary oximes--reactivation of acetylcholinesterase and butyrylcholinesterase inhibited by paraoxon
Molecules 14 :4915

Kuca K, Musilova L, Palecek J, Cirkva V, Paar M, Musilek K, Hrabinova M, Pohanka M, Karasova JZ, Jun D (2009)
Molecules 14 :4915