ArticleBiotechnology and bioprocess engineering : BBE2018
Improvement in the Reproducibility of a Paper-based Analytical Device (PAD) Using Stable Covalent Binding between Proteins and Cellulose Paper.
Article in Biotechnology and bioprocess engineering : BBE, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Is this the end of dried blood spots as we know it?Analytical science advances · 2023Article
- A colorimetric lateral flow immunoassay based on oriented antibody immobilization for sensitive detection of SARS-CoV-2.Sensors and actuators. B, Chemical · 2023Article
- Lab-on-a-chip technologies for food safety, processing, and packaging applications: a review.Environmental chemistry letters · 2022Review
- Immobilization of Proteinase K for urine pretreatment to improve diagnostic accuracy of active tuberculosis.PloS one · 2021Article
- Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning.Antibodies (Basel, Switzerland) · 2019Article
- Secondary metabolites (SMs) ofRSC advances · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paper-based analytical devices (PADs) have been widely used in many fields because they are affordable and portable. For reproducible quantitative analysis, it is crucial to strongly immobilize proteins on PADs. Conventional techniques for immobilizing proteins on PADs are based on physical adsorption, but proteins can be easily removed by weak physical forces. Therefore, it is difficult to ensure the reproducibility of the analytical results of PADs using physical adsorption. To overcome this limitation, in this study, we showed a method of covalent binding of proteins to cellulose paper. This method consists of three steps, which include periodate oxidation of paper, the formation of a Schiff base, and reductive amination. We identified aldehyde and imine groups formed on paper using FT-IR analysis. This covalent bonding approach enhanced the binding force and binding capacity of proteins. We confirmed the activity of an immobilized antibody through a sandwich immunoassay. We expect that this immobilization method will contribute to the commercialization of PADs with high reproducibility and sensitivity.
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Registered trials
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