Literature DB >> 19842944

Inactivation of acetylcholinesterase by various fluorophores.

Lilu Guo1, Alirica I Suarez, Charles M Thompson.   

Abstract

The inhibition of recombinant mouse acetylcholinesterase (rMAChE) and electric eel acetylcholinesterase (EEAChE) by seven, structurally different chromophore-based (dansyl, pyrene, dabsyl, diethylamino- and methoxycoumarin, Lissamine rhodamine B, and Texas Red) propargyl carboxamides or sulfonamides was studied. Diethylaminocoumarin, Lissamine, and Texas Red amides inhibited rMAChE with IC50 values of 1.00 microM, 0.05 microM, and 0.70 microM, respectively. Lissamine and Texas Red amides inhibited EEAChE with IC50 values of 3.57 and 10.4 microM, respectively. The other chromophore amides did not inhibit either AChE. The surprising inhibitory potency of Lissamine was examined in further detail against EEAChE and revealed a mixed-type inhibition with Ki = 11.7 microM (competitive) and Ki' = 24.9 microM (noncompetitive), suggesting that Lissamine binds to free enzyme and enzyme-substrate complex.

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Year:  2010        PMID： 19842944      PMCID： PMC3253716          DOI： 10.3109/14756360903027816

Source DB:  PubMed          Journal:  J Enzyme Inhib Med Chem        ISSN： 1475-6366            Impact factor:   5.051


  19 in total

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