Novel lactate dehydrogenase inhibitors with in vivo efficacy against Cryptosporidium parvum
Fig 2
Effect of the diverse set compounds on the catalytic activity of recombinant CpLDH protein.
Individually reconstituted compounds were used at a final concentration of 20 μM in the reaction for the reduction of pyruvate to lactate with recombinant CpLDH protein as enzyme. The mean percent inhibition of CpLDH activity by each compound was derived by dividing the mean change in optical density (ΔOD340) of the reaction after 2 min in the presence of the compound by the mean ΔOD340 of the reaction without compound, and multiplying the product by 100. The baseline mean percent inhibition of 0 (buffer) was for the reaction without compound, but with an equivalent volume of solvent used to reconstitute compound. Compounds with mean percent inhibition values greater than 0 were designated as inhibitors of the activity of CpLDH, while those with mean percent inhibition values less than 0 were classified as augmenters. Each reaction was performed in triplicate, and the data shown represents means of three independent experiments.