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. 2017 Nov 3;10(1):81–94. doi: 10.1080/19420862.2017.1389355

Figure 11.

Figure 11.

Presence of the carboxymethyl dextran matrix and constraining the Fab domain of IgG molecules by binding to antigen alters steady-state KD to FcRn. The FcRn SPR binding assay was carried out on SA and NA chips with a carboxymethyl dextran matrix, on NA coated on a C1 chip with no matrix and on IgG molecules captured on antigen for the five IgG molecules from panel 6 that vary by 1–3 amino acid residues in CDRs only on at least three experiments on a minimum of two different surfaces. Significant steady-state KD differences between IgG molecules tested with or without matrix were analyzed using an unpaired student t-test where significance is indicated as single asterisk (*) for p < 0.05.