Plasma-polymerized antifouling biochips for label-free measurement of protease activity in cell culture media
- Authors
- Park, Jisoo; Kim, Gae Baik; Lippitz, Andreas; Kim, Young Mi; Jung, Donggeun; Unger, Wolfgang E. S.; Kim, Young-Pil; Lee, Tae Geol
- Issue Date
- Feb-2019
- Publisher
- ELSEVIER SCIENCE SA
- Keywords
- Protease activity; Plasma copolymerization; Antifouling; Nonspecific adsorption; Surface plasmon resonance
- Citation
- SENSORS AND ACTUATORS B-CHEMICAL, v.281, pp.527 - 534
- Indexed
- SCIE
SCOPUS
- Journal Title
- SENSORS AND ACTUATORS B-CHEMICAL
- Volume
- 281
- Start Page
- 527
- End Page
- 534
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/15078
- DOI
- 10.1016/j.snb.2018.10.123
- ISSN
- 0925-4005
- Abstract
- We report polyethylene glycol (PEG)-grafting antifouling surfaces using a plasma copolymerized (PcP) technique to monitor protease activity in complex media. By varying the mixing ratio of the PEG and ethylenediamine (EDA) precursors, the PcP-PEG-EDA (PcP-PE) film was able to easily control surface amine density with good preservation of the internal PEG structure. We found that nonspecific protein adsorption was dramatically reduced in serum-containing media on the PcP-PE films, as opposed to that on plasma polymerized-EDA (PP-E) films without PEG. When SPR sensor chips coated with PcP-PE film were employed to detect protease activity, biotinylated luciferase probes (luciferase-peptide-biotin) on streptavidin-conjugated SPR chips enabled real-time and label-free measurement of matrix metalloproteinase activity in cell culture media. Owing to its excellent antifouling ability, this newly developed method boasts minimal nonspecific binding and can serve as a biochip platform to promote a wide range of applications in the biological field.
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