2D-Molecular homology modeling of selected Enolase enzyme for Leishmaniasis
Abstract
In present study, BLAST search was performed and an identity with Trypanosoma brueei is 79% Based upon and Pfam results Enolase- 2PTZ (protein data bank) was considered as an ideal homologue and used as a template for homology modeling due to its higher X-ray resolution at 1.65. Sequence alignment between enolase and 2PTZ was done using align 123 followed by manual modification. The final alignment was carefully evaluated and evidenced to be matching the conserved residue data for chain A of enolase in Trypanosoma brucei well Superimposing of the model was done over the template 2PTZ. Further research on the comparison of the models for the inhibitors may eluciadate the mechanism of enolase ligands interactions. This study has shown that some formation of favorable hydrogen bonds, hence it is predicated from this study that these novel compounds may act as potent inhibitors for Leishmania Enolase. These compounds may be used further for synthesis, their wet lab activity against Enolase, animal model study and clinical trials and then can be implicated for the treatment of leishmaniasis. Those models are considered to be used in designing new leads for hopefully more active compounds.
Keywords: Enolase, Leishmaniasis, Enzyme, 2D-moleculare Modeling
DOI
https://doi.org/10.22270/jddt.v8i6-s.2117References
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