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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) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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