

FOLLOWUS
a.Key Laboratory of Bionic Engineering, Ministry of Education, Jilin University, Changchun 130022, China
b.State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China
c.Jilin Province People's Hospital, Changchun 130021, China
Jie Zhao, E-mail jiezhao@jlu.edu.cn
Received:23 August 2017,
Accepted:30 August 2017,
Online First:01 December 2017,
Published:05 April 2018
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Jie Zhao, Ru Mo, Li-Mei Tian, et al. Oriented Antibody Immobilization and Immunoassay Based on Boronic Acid-containing Polymer Brush[J]. Chinese Journal of Polymer Science, 2018, 36(4): 472-478.
Jie Zhao, Ru Mo, Li-Mei Tian, et al. Oriented Antibody Immobilization and Immunoassay Based on Boronic Acid-containing Polymer Brush[J]. Chinese Journal of Polymer Science, 2018, 36(4): 472-478. DOI: 10.1007/s10118-018-2031-0.
High sensitive immunoassay platforms have gained intense attention due to their vital roles in early-stage disease diagnosis and therapeutic information feedback. Although random covalent-binding of antibody has been widely adopted in immunoassays due to its simplicity and effectiveness
it readily loses its activity and fails to exhibit high antigen-binding capacity. In this work
copolymer of zwitterionic sulfobetaine methacrylate (SBMA) and glycidyl methacrylate (GMA) brushes were immobilized onto inert polypropylene (PP)
via
surface-initiated atom transfer radical polymerization (ATRP) based on biomimetic dopamine pretreatment. Subsequently
boronic acid (BA) groups were covalently bonded
via
active GMA units
followed by the introduction of oriented immobilization of antibody. Owing to the oriented immobilization of antibody facilitated by BA groups in polymer brush
the bioactivity of antibody is well preserved
which endows the surface with significantly enhanced antigen-binding capacity. Moreover
the existence of SBMA segments in polymer brushes renders the surface high resistance to nonspecific protein adsorption
significantly alleviating the signal interference of antigen recognition. This strategy could find potential applications in developing high sensitive immunoassay platforms based on the different substrates.
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