Chumphukam_2014_Molecules_19_4986

Reference

Title : High efficiency acetylcholinesterase immobilization on DNA aptamer modified surfaces - Chumphukam_2014_Molecules_19_4986
Author(s) : Chumphukam O , Le TT , Cass AE
Ref : Molecules , 19 :4986 , 2014
Abstract :

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.

PubMedSearch : Chumphukam_2014_Molecules_19_4986
PubMedID: 24756130

Related information

Citations formats

Chumphukam O, Le TT, Cass AE (2014)
High efficiency acetylcholinesterase immobilization on DNA aptamer modified surfaces
Molecules 19 :4986

Chumphukam O, Le TT, Cass AE (2014)
Molecules 19 :4986