Liquid crystal sensor for the detection of acetylcholine using acetylcholinesterase immobilized on a nanostructured polymeric surface
- Authors
- Han, Gyeo-Re; Jang, Chang-Hyun
- Issue Date
- Oct-2015
- Publisher
- SPRINGER
- Keywords
- Liquid crystals; Polymeric surfaces; Acetylcholine; Acetylcholinesterase; Acetylcholinesterase inhibitor
- Citation
- COLLOID AND POLYMER SCIENCE, v.293, no.10, pp.2771 - 2779
- Journal Title
- COLLOID AND POLYMER SCIENCE
- Volume
- 293
- Number
- 10
- Start Page
- 2771
- End Page
- 2779
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/10074
- DOI
- 10.1007/s00396-015-3648-y
- ISSN
- 0303-402X
- Abstract
- In this study, we report on a label-free biosensor for the detection of acetylcholine (ACh) and an acetylcholinesterase (AChE) inhibitor, utilizing liquid crystals (LCs) on a polymeric surface with periodic nanostructures. The polymeric nanostructures, which hold sinusoidal anisotropic patterns, were fabricated by a sequential process of poly(dimethylsiloxane) buckling and replication of these patterns on a poly(urethane acrylate) surface where a film of gold was deposited. AChE was then covalently immobilized onto the gold surface. Optical images of nematic 4-cyano-4'-pentylbiphenyl (5CB) revealed that it aligned parallel to the plane of the enzyme-decorated surface. However, AChE-mediated hydrolysis of ACh resulted in a plume of choline, acetate, and unreacted ACh, which in turn produced a distinctive optical transition of 5CB (from uniform to random) by masking the anisotropic surface topography. The hydrolysis of ACh was inhibited in the presence of a carbamate insecticide (AChE inhibitor), which prevented the orientational transition of 5CB by decreasing the enzymatic activity of AChE. These results suggest that this LC-based enzymatic sensor is highly sensitive to ACh and the AChE inhibitor, with a detection limit of 10 and 1 nM, respectively. This study demonstrates that polymeric surfaces with continuous wavy features can be used as LC-based biosensors to amplify the existence of ACh and an AChE inhibitor without labeling or an additional amplification strategy.
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