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Molecules 2014, 19(4), 4986-4996; doi:10.3390/molecules19044986

High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces

,  and *
Department of Chemistry, Imperial College, London SW7 2AZ, UK
* Author to whom correspondence should be addressed.
Received: 26 February 2014 / Revised: 8 April 2014 / Accepted: 11 April 2014 / Published: 21 April 2014
(This article belongs to the Section Molecular Diversity)
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We report here the in vitro selection of DNA aptamers for electric eel acetylcholinesterase (AChE). One selected aptamer sequence (R15/19) has a high affinity towards the enzyme (Kd = 157 ± 42 pM). Characterization of the aptamer showed its binding is not affected by low ionic strength (~20 mM), however significant reduction in affinity occurred at high ionic strength (~1.2 M). In addition, this aptamer does not inhibit the catalytic activity of AChE that we exploit through immobilization of the DNA on a streptavidin-coated surface. Subsequent immobilization of AChE by the aptamer results in a 4-fold higher catalytic activity when compared to adsorption directly on to plastic.
Keywords: aptamers; acetylcholinesterase; immobilization aptamers; acetylcholinesterase; immobilization
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Chumphukam, O.; Le, T.T.; Cass, A.E.G. High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces. Molecules 2014, 19, 4986-4996.

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