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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

From: Towards development of aptamers that specifically bind to lactate dehydrogenase of Plasmodium falciparum through epitopic targeting

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]
  1. K D estimated apparent dissociation constant (M) of the aptamer-target complex, Γ max 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
  2. * Wald test produced a probability, p of < 0.05 for this parameter