Molecular Docking Study of the Interactions between Plasmodium falciparum Lactate Dehydrogenase and 4-Aminoquinoline Hybrids
2020
Malaria is a potentially deadly disease with many anti-malarial drugs have been rendered ineffective due to
Plasmodium falciparum resistance concern. Plasmodium falciparum lactate dehydrogenase (PfLDH) enzyme is a crucial
malaria parasite enzyme involved in the glycolytic pathway, thus, has been considered as a potential molecular
target. Initially, molecular docking was performed using AutoDock Vina, Molegro Virtual Docker, and CDOCKER
software to investigate the molecular interactions of 4-aminoquinoline antimalarial hybrids compounds with PfLDH
enzyme. All ten 4-aminoquinoline hybrids derivatives docked to the PfLDH binding site. The results showed that these
compounds exhibited either comparable or higher binding affinity than the reference drug chloroquine, amodiaquine,
and hydroxychloroquine. Visually, some of the compounds possessed functional binding interactions, possibly due to
their similar structural conformation and binding interactions of chloroquine in the binding site. Apart from that, the
docking results also suggest that these compounds potentially promote additional hydrogen-bonding interactions with
the residues in the binding site. Interestingly, the compounds also predicted to interact with essential PHE52, VAL26,
ILE54, ILE119, and ALA98 residues, which are required to act as a competitive inhibitor for this glycolytic enzyme.
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