Table 1 Inhibitors Structure, LmTXNPx Inhibiton Assay and KDs (μM) Calculated by Surface Plasmon Resonance

From: Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking

Cpds

R1

R2

R3

HRP inhib.

(ΔA/ΔA0) × 100a

KD (μM)

1

H

F

6,7-diOMe

No

52 ± 10%

290 ± 13

2

NO2

F

6,7-diOMe

No

37 ± 9%

172 ± 6

3

NH2

F

6,7-diOMe

No

44 ± 6%

354 ± 12

4

NMe2

F

6,7-diOMe

Nd

Nd

156 ± 5

5

I

F

6,7-diOMe

No

71 ± 6%

281 ± 11

6

Ph

F

6,7-diOMe

No

75 ± 9%

52 ± 1

7

H

F

6-OMe

No

60 ± 7%

47 ± 1

8

H

F

H

No

45 ± 15%

104 ± 4

9

H

H

6,7-diOMe

Yes

-

74 ± 3

10

H

Cl

6,7-diOMe

Yes

-

63 ± 3

11

H

Br

6,7-diOMe

No

37 ± 20%

112 ± 4

12

-

-

-

No

93 ± 6%

39 ± 1

  1. aHRP 2 μM was exposed to H2O2 0.25 μM in sodium phosphate buffer pH 7.4 and 25°C, in the presence of 2.5 μM LmTXNPx and 100 μM inhibitors. The residual activity of HRP was calculated as ΔA/ΔA0 where ΔA0 is the difference in absorbance between HRP and HRP-I (ΔA0 = 0.04 ± 0.01) and ΔA is the difference in absorbance between HRP and HRP-I in the presence of LmTXNPx and inhibitors.
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