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A Bioinformatics Approach for Homology Modeling and Binding Site Identification of Triosephosphate Isomerase from Plasmodium falciparum 3D7. | LitMetric

AI Article Synopsis

  • Malaria is a significant public health issue, with drug-resistant malarial parasites leading to the urgent need for new treatment targets.
  • Researchers focused on Plasmodium falciparum 3D7, which relies solely on glycolysis for energy due to its lack of a functional tricarboxylic acid cycle, and studied its enzymes as potential drug targets.
  • The tertiary structure of the enzyme triose phosphate isomerase was modeled using advanced techniques, revealing promising characteristics that could make it a suitable target for future vaccine development, pending further experimentation.

Article Abstract

Malaria is a major public health concern, and malarial parasites have developed resistance against the commonly available drugs. So now a days it is a major concern to find out a new target for drug therapy. Plasmodium falciparum 3D7, one of the strains of plasmodium species also lacks in a functional tricarboxylic acid cycle and solely dependent on glycolysis for its energy supply like other plasmodium species. Although enzymes of malarial parasite have been considered as potential antimalarial drug targets, a little is known about their structural biology. The tertiary structure of triose phosphate isomerase of P. falciparum 3D7 was determined by means of homology modeling through multiple alignment followed by intensive optimization and validation. The modeling was done by Swiss-Model Workspace. The obtained model was verified with the structure validation programs such as, PROCHECK, Verify3D, and QMEAN for reliability. The verify3D value of 0.69 indicates that the environment profile of the model is good. A self-optimized prediction method with alignment or SOPMA is employed for calculation of the secondary structural features of triose phosphate isomerase. The secondary structure indicates that the predicted 3D structure of triosephosphate isomerase of P. falciparum 3D7 contains 48.37% α-helix, 29.27% random coil, and 16.67% extended strand. Active site determination through CASTp suggests that this protein can be utilized as a potential drug target. However, these will further be tested by wet lab studies for a targeted vaccine design against P. falciparum 3D7.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573378PMC
http://dx.doi.org/10.4103/0975-1483.104370DOI Listing

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