| 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 |
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