Binding affinities of chalcones, flavonols, sterols, sapogenins and carbazoles downloaded from PubChem on antimalaria targets

Malaria remains a persistent health challenge in Africa, particularly in Nigeria, where it accounts for the highest mortality rates. The increasing resistance of Plasmodium parasites to conventional antimalarial drugs necessitates the exploration of novel therapeutic agents. This study focuses on the in silico screening of 938 chalcones, 817 flavonoids, 622 sterols, 815 sapogenins, and 1725 carbazoles sourced from the PubChem database (https://pubchem.ncbi.nlm.nih.gov/). Target proteins, including Plasmepsin IV from P. falciparum in complex with pepstatin A(1LS5), plasmepsin II from Plasmodium falciparum (3F9Q), histo-aspartic protease (HAP) from Plasmodium falciparum (3QVI), Plasmodium falciparum dihydroorotate dehydrogenase (6GJG), Falcipain-2 (3BPF), Falcipain-3 (3BPM), and plasmodium falciparum lactate dehydrogenase (1CET) were obtained from the Protein Data Bank (http://www.rcsb.org/pdb/home/home.do). Molecular docking simulations were performed using Autodock Vina (https://vina.scripps.edu/) to evaluate the binding affinities of the ligands with each target protein. Molecular and pharmacokinetic properties of the ligands were assessed using resources from Molinspiration (https://www.molinspiration.com/cgi-bin/properties) and pkcsm (http://biosig.unimelb.edu.au/pkcsm/prediction) websites, respectively. The results, including binding affinities and biological properties, are presented in tabular form. This study lays the foundation for identifying potential antimalarial compounds through computational methodologies.