Pregled bibliografske jedinice broj: 627
Synthesis of quinuclidine-imidazole derivatives and their interaction with acetylcholinesterase
Synthesis of quinuclidine-imidazole derivatives and their interaction with acetylcholinesterase // Hrvatsko biokemijsko društvo - Svečani sastanak hrvatskih biokemičara uz 20. obljetnicu osnutka društva, Zagreb, (Sažeci postera, ISBN 953-6256-19-3) / Flögel, Mirna (ur.).
Zagreb: Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 1996. (poster, domaća recenzija, sažetak, znanstveni)
CROSBI ID: 627 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Synthesis of quinuclidine-imidazole derivatives and their interaction with acetylcholinesterase
Autori
Simeon-Rudolf, Vera ; Reiner, Elsa ; Škrinjarić-Špoljar, Mira ; Buntić, Anđelka ; Primožič, Ines
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Hrvatsko biokemijsko društvo - Svečani sastanak hrvatskih biokemičara uz 20. obljetnicu osnutka društva, Zagreb, (Sažeci postera, ISBN 953-6256-19-3)
/ Flögel, Mirna - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 1996
Skup
Hrvatsko biokemijsko društvo-Svečani sastanak hrvatskih biokemičara uz 20. obljetnicu osnutka društva
Mjesto i datum
Zagreb, Hrvatska, 18.10.1996. - 19.10.1996
Vrsta sudjelovanja
Poster
Vrsta recenzije
Domaća recenzija
Ključne riječi
quinuclidine compounds; acetylcholinesterase; reversible inhibition; protection in phosphorylation; VX; soman
Sažetak
Three compounds: N-methyl 3-oxo quinuclidinium iodide (I), 2-hydroxyiminomethyl 1, 3-dimethylimidazolium iodide (II) and this two compounds linked by a threemethylene link (III) were synthetised and studied as reversible inhibitors of human erythrocyte acetylcholinesterase (AChE) and as protectors against phosphorylation of the enzyme by the warfare agents Soman and VX. All the three compounds were found to be reversible inhibitors of AChE. The substrate was acetylthiocholine. The enzyme/inhibitor dissociation constants for the catalytic site were evaluated at low substrate concentrations up to 1.0 mM ; the compound II showed the highest affinity. At substrate concentrations above 1 mM inhibition by compound I revealed a second binding site. Inhibition at high substrate concentrations by the compounds II and III could not be measured due to a non-enzymic hydrolysis of the substrate by the oxime. All three compounds protected AChE against phosphorylation by soman and VX. Protection by compound I was enhanced through interaction of this compound with the allosteric binding site.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Kliničke medicinske znanosti
POVEZANOST RADA
Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb,
Prirodoslovno-matematički fakultet, Zagreb
