In diseases such as cancer, cellular parasite infections (malaria, sleeping sickness), and bacterial infections that depend on glycolysis for cellular energy and supply of metabolic precursors, inhibition of glycolysis by targeting aldolase represents a novel form of therapy. A nanomolar affinity inhibitor was synthesized from structure-assisted drug design by a collaborator, Dr. C. Blonski at Toulouse. The compound is the most potent inhibitor of mammalian aldolases tested to date. Molecular dynamics was used to analyze the atomic interactions made by the inhibitor with aldolase to understand its tight binding affinity. The molecular trajectory revealed atomic geometries in the inhibitor-aldolase complex that were consistent with covalent reaction by the inhibitor with aldolase explaining the observed tight binding inhibition. An isomer of this lead compound is highly specific against aldolase from protozoan parasites causing sleeping sickness.