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Arhiv za higijenu rada i toksikologiju, Vol.58 No.2 Svibanj 2007.

Izvorni znanstveni članak
https://doi.org/10.2478/v10004-007-0013-7

Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes

Zrinka Kovarik
Maja Čalić
Goran Šinko
Anita Bosak

Puni tekst: engleski, pdf (253 KB) str. 201-209 preuzimanja: 723* citiraj
APA 6th Edition
Kovarik, Z., Čalić, M., Šinko, G. i Bosak, A. (2007). Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes. Arhiv za higijenu rada i toksikologiju, 58 (2), 201-209. https://doi.org/10.2478/v10004-007-0013-7
MLA 8th Edition
Kovarik, Zrinka, et al. "Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes." Arhiv za higijenu rada i toksikologiju, vol. 58, br. 2, 2007, str. 201-209. https://doi.org/10.2478/v10004-007-0013-7. Citirano 16.11.2018.
Chicago 17th Edition
Kovarik, Zrinka, Maja Čalić, Goran Šinko i Anita Bosak. "Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes." Arhiv za higijenu rada i toksikologiju 58, br. 2 (2007): 201-209. https://doi.org/10.2478/v10004-007-0013-7
Harvard
Kovarik, Z., et al. (2007). 'Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes', Arhiv za higijenu rada i toksikologiju, 58(2), str. 201-209. doi: https://doi.org/10.2478/v10004-007-0013-7
Vancouver
Kovarik Z, Čalić M, Šinko G, Bosak A. Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes. Arh Hig Rada Toksikol. [Internet]. 2007 [pristupljeno 16.11.2018.];58(2):201-209. doi: https://doi.org/10.2478/v10004-007-0013-7
IEEE
Z. Kovarik, M. Čalić, G. Šinko i A. Bosak, "Structure-Activity Approach in the Reactivation of Tabun-Phosphorylated Human Acetylcholinesterase with Bispyridinium para-Aldoximes", Arhiv za higijenu rada i toksikologiju, vol.58, br. 2, str. 201-209, 2007. [Online]. doi: https://doi.org/10.2478/v10004-007-0013-7

Sažetak
We investigated interactions of bispyridinium para-aldoximes N,N’-(propano)bis(4-hydroxyiminomethyl) pyridinium bromide (TMB-4), N,N’-(ethano)bis(4-hydroxyiminomethyl)pyridinium methanosulphonate (DMB-4), and N,N’-(methano)bis(4-hydroxyiminomethyl)pyridinium chloride (MMB-4) with human erythrocyte acetylcholinesterase phosphorylated by tabun. We analysed aldoxime conformations to determine the flexibility of aldoxime as an important feature for binding to the acetylcholinesterase active site. Tabun-inhibited human erythrocyte acetylcholinesterase was completely reactivated only by the most flexible bispyridinium aldoxime - TMB-4 with a propylene chain between two rings. Shorter linkers than propylene (methylene or ethylene) as in MMB-4 and DMB-4 did not allow appropriate orientation in the active site, and MMB-4 and DMB-4 were not efficient reactivators of tabun-phosphorylated acetylcholinesterase. Since aldoximes are also reversible inhibitors of native acetylcholinesterase, we determined dissociation constants and their protective index against acetylcholinesterase inactivation by tabun.

Ključne riječi
antidotes; nerve agents; organophosphorus compounds

Hrčak ID: 12902

URI
https://hrcak.srce.hr/12902

[hrvatski]

Posjeta: 1.045 *