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Fig. 2 | Journal of Hematology & Oncology

Fig. 2

From: A non-internalised CD38-binding radiolabelled single-domain antibody fragment to monitor and treat multiple myeloma

Fig. 2

a (i) Biolayer interferometry sensorgrams from a dilution series of sdAb #2F8 from 50 to 2.5 nM to assess its binding to the CD38. The blue curves represent the experimental kinetics, and the red ones represent fit curves. (ii) Summary of the different binding parameters for the sdAbs studied and the sdAb 2F8 conjugated to the chelator DTPA used in radiolabelling with 111In and 177Lu. The data are expressed as mean ± SD (n = 4). b (i) Competitive binding between daratumumab and sdAbs (#2F8, #551, #375 or #1053) for binding to the CD38, (ii) data obtained for competitor sdAb #1053 and daratumumab, where no additional signal is observed upon addition of sdAb on mAb-CD38 complex (dark green) and vice versa (light green), (iii) similar results obtained for the sdAb #375 (addition of sdAb on mAb-CD38 complex in black and the reverse in grey), (iv) partial-competitor sdAb #551 and daratumumab where an additional signal is observed upon the addition of mAb on sdAb-CD38 complex but with a lower amplitude than when it was immobilised first (light blue). A decrease in signal after addition of sdAb on mAb-CD38 complex is observed (dark blue), which may indicate loss of binding for daratumumab. Finally, (v) non-competitor sdAb #2F8 and daratumumab, where no competition is observed. The two proteins are able to bind the receptor without impacting the signal amplitude, regardless of the order of addition

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