Skip to main content
. 2021 Feb 16;12:1063. doi: 10.1038/s41467-021-21221-4

Table 1.

Dissociation constants of antibody Fabs and fold-changes in apparent affinity obtained from ITC.

mAb Kd to NPNA2 (nM) Kd to NPNA4 (nM) Kd to NPNA6 (nM) Mean Kd fold-change NPNA2 vs NPNA6
239 641 ± 38 20 ± 2 10 ± 1 64
311 152 ± 11 14 ± 5 19 ± 4 8
337 1523 ± 11 71 ± 1 59 ± 14 26
356 8272 ± 1284 82 ± 18 30 ± 6 276
364 47 ± 2 28 ± 2 27 ± 3 2
395 6152 ± 196 1423 ± 404 999 ± 231 6
mAb Kd to NPNA2 (nM) Kd to NPNA4 (nM) Kd to NPNA6 (nM) Mean Kd fold-change NPNA4 vs. NPNA6a
224 14245 ± 4507 126 ± 14 141 ± 8 1
366 1348 ± 110 1770 ± 82 479 ± 17 4
397 2743 ± 156 255 ± 10 92 ± 8 3
399 13345 ± 2017 5922 ± 1122 94 ± 30 63
317 132 ± 62 70 ± 12 111 ± 23 1

aThe fold-change calculation for these two sets of antibodies is between NPNA4 and NPNA6 as it was shown by the crystal structures that their minimal epitopes are NPNA3. Thus, the comparison between NPNA2 and NPNA6 would not be appropriate here.