A cationic surfactant-decorated liquid crystal sensing platform for simple and sensitive detection of acetylcholinesterase and its inhibitor
In this paper, construction of the liquid crystal (LC)-based sensing platform for simple and sensitive detection of acetylcholinesterase (AChE) and its inhibitor using a cationic surfactant-decorated LC interface was demonstrated. A change of the optical images of LCs from bright to dark appearance...
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Veröffentlicht in: | Biosensors & bioelectronics 2015-10, Vol.72, p.25-30 |
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Sprache: | eng |
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Zusammenfassung: | In this paper, construction of the liquid crystal (LC)-based sensing platform for simple and sensitive detection of acetylcholinesterase (AChE) and its inhibitor using a cationic surfactant-decorated LC interface was demonstrated. A change of the optical images of LCs from bright to dark appearance was observed when the cationic surfactant, myristoylcholine chloride (Myr), was transferred onto the aqueous/LC interface, due to the formation of a stable surfactant monolayer at the interface. A dark-to-bright change of the optical appearance was then observed when AChE was transferred onto the Myr-decorated LC interface. The sensitivity of this new type of LC-based sensor is 3 orders of magnitude higher in the serum albumin solution than that only in the buffer solution. Noteworthy is that the AChE LC sensor shows a very high sensitivity for the detection of the enzyme inhibitor, which is around 1fM. The constructed low-cost LC-based sensor is quite simple and convenient, showing high promise for label-free detection of AChE and its inhibitors.
•A novel approach to detect acetylcholinesterase and its inhibitor using liquid crystals.•The cationic surfactant-decorated liquid crystal interface is used as the sensing platform.•This low-cost and label-free strategy is quite simple and highly sensitive.•The detection limit of the enzyme is around 0.000827U/mL in a serum albumin solution.•The detection limit of the enzyme inhibitor is around 1fM. |
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ISSN: | 0956-5663 1873-4235 |
DOI: | 10.1016/j.bios.2015.05.001 |