High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces
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), how...
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-04-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/19/4/4986 |
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| author | Orada Chumphukam Thao T. Le Anthony E. G. Cass |
| author_facet | Orada Chumphukam Thao T. Le Anthony E. G. Cass |
| author_sort | Orada Chumphukam |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-19T22:24:57Z |
| format | Article |
| id | doaj.art-0799101bd305437a8b366c7fae8c9921 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-19T22:24:57Z |
| publishDate | 2014-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-0799101bd305437a8b366c7fae8c99212022-12-21T20:03:32ZengMDPI AGMolecules1420-30492014-04-011944986499610.3390/molecules19044986molecules19044986High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified SurfacesOrada Chumphukam0Thao T. Le1Anthony E. G. Cass2Department of Chemistry, Imperial College, London SW7 2AZ, UKDepartment of Chemistry, Imperial College, London SW7 2AZ, UKDepartment of Chemistry, Imperial College, London SW7 2AZ, UKWe 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.http://www.mdpi.com/1420-3049/19/4/4986aptamersacetylcholinesteraseimmobilization |
| spellingShingle | Orada Chumphukam Thao T. Le Anthony E. G. Cass High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces Molecules aptamers acetylcholinesterase immobilization |
| title | High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces |
| title_full | High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces |
| title_fullStr | High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces |
| title_full_unstemmed | High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces |
| title_short | High Efficiency Acetylcholinesterase Immobilization on DNA Aptamer Modified Surfaces |
| title_sort | high efficiency acetylcholinesterase immobilization on dna aptamer modified surfaces |
| topic | aptamers acetylcholinesterase immobilization |
| url | http://www.mdpi.com/1420-3049/19/4/4986 |
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