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![[Figure 2]](ag5062fig2mag.jpg)
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Figure 2
Characterization of nanobody binding. (a) Titration ELISAs using 50 nM SmCD1 immobilized in wells of a 96-well plate to assess the binding of purified nanobody, detected using anti-camelid VHH-HRP. Data shown represent single measurements from small-scale expressed material used for initial candidate prioritization. (b) Biolayer interferometry using streptavidin biosensors loaded with 50 nM biotinylated SmCD1 binding to Nb10C9. Association occurred during the first 600 s; samples were then transferred to a buffer-containing well to measure dissociation for a further 600 s. Values shown in the table are weighted averages calculated from n = 3 technical replicates. Error values represent standard error of the mean. (c) Titration ELISA of Nb10C9 bound to SmCD1, human cathepsin D (hCD) or human cathepsin E (hCE). (d) Amino-acid sequence of Nb10C9 with CDRs shown in bold (IMGT numbering; Giudicelli et al., 2011  ), with secondary structures of Nb10C9 depicted along the top of the sequence. Green digits indicate disulfide bridges. |
![[Figure 2]](ag5062fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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