Abstract
Aim. To evaluate polymorphism of dinitroaniline/phosphorothioamidate binding site in α-tubulin molecules from Plasmodium species (P. falciparum, P. vivax, P. ovale, and P. malariae) and strains discovered in India. Methods. Literature and database search. Bioinformatical comparison of protein sequences and structures. Multiple sequence alignment, phylogenetic profiling, protein structure modeling, etc. Results. 14 complete sequences of α-tubulin from four Plasmodium species were selected from UniProtKB. Despite certain differences in complete sequences of α-tubulin molecules from different Plasmodium species and strains, sites of their interaction with dinitroaniline and phosphorothioamidate compounds were shown to be identical. Conclusions. Complete identity of dinitroaniline/phosphorothioamidate binding sites in all studied isotypes of α-tubulin molecules from P. falciparum, P. vivax, P. ovale, and P. malariae was confirmed. This suggests identity of the ligand-protein interaction mechanism and similar destabilizing effect of dinitroaniline and phosphorothioamidate compounds on microtubules of all Plasmodium species officially registered in India.
 Keywords: malaria, Plasmodium, α-tubulin, dinitroanilines, phosphorothioamidates, binding site.
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