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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