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Fig. 3 | Journal of Nanobiotechnology

Fig. 3

From: A potent synthetic nanobody with broad-spectrum activity neutralizes SARS-CoV-2 virus and the Omicron variant BA.1 through a unique binding mode

Fig. 3

Affinity maturation of C5 clone by phage display led to the identification of the C5G2 clone A The C5 clone was used as the template to generate an optimization library with mutations at all CDRs. Panning of this library against RBD resulted in ten C5 variants. The CDR regions of these ten clones were aligned. The alignments represented by Weblogo are shown underneath each CDR region. B The C5G2 variant was purified from the E. coli host and resolved by SDS‒PAGE. C Binding curve of the C5G2 protein to RBD in the BLI assay. The binding affinity increased from 18 nM to 1.62 nM. D Size exclusion chromatography (SEC) profile of C5G2 protein resolved in a Tosho TSKgel G3000SW column

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