Screening of Oxamic Acid Similar 3D Structures as Candidate Inhibitor Plasmodium falciparum L-Lactate Dehydrogenase of Malaria Through Molecular Docking

The rise of strains of malarial parasite resistant to customary medication treatment has invigorated ongoing looks for antimalarials with novel methods of activity. A contender for this approach in the battle against malaria is the L-lactate dehydrogenase from Plasmodium falciparum (PfLDH). P. falciparum LDH is a fundamental catalyst for vitality age inside the parasite. Lactate dehydrogenase (PfLDH) is a key chemical in the glycolytic pathway of P. falciparum, lessening pyruvate to lactate with the guide of NADH. Oxamate is a non competitive inhibitor of the binding of pyruvate to LDH, and a few oxamic derivates have been created as lead mixes for specific PfLDH inhibitors like 1LDG. The purpose of our study was to screen for oxamic acid-like structures as PfLDH inhibitors by docking method so as to enrich the inhbitor alternative PfLDH and to discover a lead intensify that presentations specific action against PfLDH. Our method by preparation of 3D structure of 1LDG obtained from RCSB PDB (Protein Data Bank) then ligand removed from the structure of oxamic acid by using PyMol Software, new ligands oxamic acid-like structures are obtained from the Pubchem open chemistry database website, virtual screening and docking by Pyrx, and visualization by PyMol software. In this study it was found that the binding affinity of 2-Oxopropanehydrazide was the largest with a value of -5.2 Kcal/mol, but in this case only 2,2-diffluoro-2-hydroxyacetic acid is a candidate inhibitor that occupies a region close to oxamate even attached to NADH. In each of the best ligand results that the rmsd/ub and rmsd/ib value are 0.