Article citations

    Morris, G.M., Huey, R., Lindstrom, W., Sanner, M.F., Belew, R.K., Goodsell, D.S. and Olson, A.J. (2009) AutoDock4 and AutoDockTools4: Automated Docking with Selective Receptor Flexiblity. Journal of Computational Chemistry, 30, 2785-2791.

has been cited by the following article:

  • TITLE: <i>In Silico</i> Evaluation of Anti-Malarial Agents from <i>Hoslundia opposita</i> as Inhibitors of <i>Plasmodium falciparum</i> Lactate Dehydrogenase (P<i>f</i>LDH) Enzyme
  • AUTHORS: Daniel M. Shadrack, Stephen S. Nyandoro, Joan J. E. Munissi, Egid B. Mubofu
  • KEYWORDS: P<i>f</i>LDH, Hoslundin, Hoslundal, Hoslunddiol, Anti-Malarial, Docking
  • JOURNAL NAME: Computational Molecular Bioscience DOI: 10.4236/cmb.2016.62002 Jul 06, 2016
  • ABSTRACT: Malaria has continued to be a health and economic problem in Africa and the world at large. Many anti-malarial drugs have been rendered ineffective due to the emergence of resistant strains of Plamodium falciparum. A key malaria parasite enzyme in glycolytic pathway, P. falciparum lactate dehydrogenase (PfLDH) is specially targeted for anti-malarial drugs development. Thus, the aim of this investigation was to determine the in silico inhibition effects of antimalarial compounds from Hoslundia opposita Vahl. namely hoslundin, hoslundal and hoslunddiol on PfLDH enzyme. The compounds were docked to the three-dimensional structure of PfLDH as enzyme using AutoDock Vina in PyRx virtual screening software. Binding affinity and position of the inhibitors were evaluated using PyMol software. The PfLDH enzyme showed two binding sites: the cofactors binding site (Site A) and secondary binding site (Site B). In the absence of the cofactor all ligands showed higher affinity than NADH, and were bound to the cofactors binding site (Site A). When docked in the presence of the cofactor, site B was the preferred binding site. Binding to cofactor site with higher binding energy than NADH suggests that these ligands could act as preferential competitive inhibitors of PfLDH. However, the binding to site B also suggests that they may be non-competitive allosteric inhibitors. Amino acid residues Gly99, Asn140, Phe100 and Thr97 were indicated to form hydrogen bonds with Hoslundin. Hoslunddiol showed hydrogen bonding with Thr97 and Met30, while Hoslundal formed hydrogen bond with Thr101 and Asn140.