Human malaria, one of the most striking, reemerging infectious diseases, is caused by several typesof
Plasmodium parasites. As the parasite digests hemoglobin in human red blood cells, the heme byproduct crystallizesinto micron-sized malaria-pigment (hemozoin). Making use of a recently reported powder-crystal structuredetermination of synthetic hemozoin (
-hematin), we describe here its theoretical growth form and show it to besimilar in habit and form to that of natural hemozoin. With this information, we propose a noncovalent binding sitefor the quinoline drug family at the end face of the fastest-growing direction of
-hematin. This adsorption mechanismis examined in terms of crystal growth inhibition vis-à-vis published data. The surface binding site elucidates thedifference in activity of various quinolines, revealing the importance of the different quinoline functionalities. Theinterplay between molecular chirality of quinolines and the chirality of centrosymmetric
-hematin crystal faces isanalyzed in terms of crystal growth inhibition. We additionally propose a molecular isomerism of the crystallinebuilding blocks, with implications on quinoline surface binding, as well as on nucleation and size of
-hematin crystals.