A highly sensitive electrochemiluminescence method for abrin detection by a portable biosensor based on a screen-printed electrode with a phage display affibody as specific labeled probe
- PMID: 34854959
- DOI: 10.1007/s00216-021-03735-4
A highly sensitive electrochemiluminescence method for abrin detection by a portable biosensor based on a screen-printed electrode with a phage display affibody as specific labeled probe
Abstract
Abrin is a highly toxic ribosome-inactivating protein, which could be used as a biological warfare agent and terrorist weapon, and thus needs to be detected efficiently and accurately. Affibodies are a new class of engineered affinity proteins with small size, high affinity, high stability, favorable folding and good robustness, but they have rarely played a role in biological detection. In this work, we establish a novel electrochemiluminescence (ECL) method for abrin detection with a phage display affibody as the specific probe for the first time, to our knowledge, and a portable biosensor based on a screen-printed electrode (SPE) as the testing platform. On the basis of the double antibody sandwich structure in our previous work, we used a phage display affibody instead of monoclonal antibody as a new specific labeled probe. Due to numerous signal molecules labeled on M13 phages, significant signal amplification was achieved in this experiment. Under optimized conditions, a linear dependence was observed from 0.005 to 100 ng/mL with a limit of detection (LOD) of 5 pg/mL. This assay also showed good reproducibility and specificity, and performed well in the detection of simulated samples. Considering its high sensitivity, interference resistance and convenience, this new biosensing system based on phage display affibodies and a portable ECL biosensor holds promise for in situ detection of toxins and pollutants in different environments.
Keywords: Abrin; Affibody; Electrochemiluminescence biosensor; Phage display technology; Screen-printed electrode.
© 2021. Springer-Verlag GmbH Germany, part of Springer Nature.
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