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Fig. 3 | Journal of Biological Engineering

Fig. 3

From: Development of anti-aflatoxin B1 nanobodies from a novel mutagenesis-derived synthetic library for traditional Chinese medicine and foods safety testing

Fig. 3

Characterization of anti-AFB1 nanobodies isolated from SynaGG library. A The eluted number of anti-AFB1 library phages was calculated after each round of panning. The wild-type M13 phage was a negative control. B Test of the binding reactivity of four representative nanobodies at the same concentration of 10 μg/mL to AFB1-BSA and MTX-BSA. BSA was used as a negative antigen control, and 3QXV denotes the original template nanobody that can recognize MTX. C Serial dilution on the two nanobodies (left: A1; right: F2) to test the binding reactivity to AFB1-BSA and AFB1-OVA. D A competitive inhibition assay determined the binding specificity of the nanobodies (nb A1 and nb F2) against the AFB1 molecule. The amount of bound nanobody in the presence of a free AFB1 inhibitor was measured and expressed as a percentage of the binding of the nanobody in the absence of an inhibitor. B and B0 denote the amount of bound nanobody in the presence and absence of the inhibitor, respectively

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