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. 2018 May 3;17:191. doi: 10.1186/s12936-018-2336-z

Table 2.

KD values for aptamers LDHp 1, LDHp 11, rLDH 4, rLDH 7, rLDH 15, C7 and pL1 binding to immobilized proteins, rPfLDH and rPvLDH determined using ELONA

Aptamer Apparent affinity constant, KD (nM) ± SE References
rPfLDH rPvLDH
KD Γmax KD Γmax
C7 NR NR NR NR This work
LDHp 1 927.3 ± 915.0 0.068 ± 0.039 CNM > 1000 0.230 ± 0.106 This work
LDHp 11 321.2 ± 82.5* 0.135 ± 0.014* 37.0 ± 41.4
CNM
0.097 ± 0.020* This work
rLDH 4 691.6 ± 393.6 0.191 ± 0.057* 444. 9 ± 144.3* 0.364 ± 0.049* This work
rLDH 7 39.9 ± 15.7* 0.180 ± 0.014* 26.3 ± 3.2* 0.283 ± 0.050* This work
rLDH 15 80.7 ± 17.1* 0.129 ± 0.007* 268.7 ± 67.2* 0.501 ± 0.429* This work
pL1 159.5 ± 167.8
CNM
0.022 ± 0.005* 79.2 ± 12.7* 0.209 ± 0.010* This work
38.7 ± 1.3 16.8 ± 0.6 [20]
6.2 2.9 [24]
2008s 42.0–59.0 [23]
43.0 NR [24]

KD estimated apparent dissociation constant (M) of the aptamer-target complex, Γmax estimated maximal assay response for the aptamer-target complex, CNM could not model—positive binding occurred, but no valid modelled KD was obtained, CNM > 1000 could not model—linear dependence indicates that apparent KD of a target did not fall within the tested concentration range i.e. KD > 1000 nM, NR no response—no evidence of binding, relative to the baseline assay response

* Wald test produced a probability, p of < 0.05 for this parameter