| dc.description.abstract | The high incidence of Tuberculosis infection and its devastating effects on the health sector worldwide that is being brought about by increased number of resistant strains of Mycobacterium tuberculosis has triggered several attempts to truncate the epidemic as available drugs are not adequately effective due to increased resistance. New advances in In-silico approaches have propelled studies into bioactive compounds such as Antimicrobial peptides against several Mycobacterium tuberculosis components including the MmpL3. Peptides represent excellent features as potential anti-MmpL3 agents due to better binding energies, safety (nontoxic), and desirable physiochemical parameters. In the current study,14 antibacterial peptides known to inhibit various bacteria, were computationally screened, the top two designed and docked against the MmpL3 of Mycobacterium tuberculosis. In the primary screening, 14 peptide sequences were found to be naturally occurring, well characterized, with < 50 amino acid residues. Further screening involved generation of peptide motifs from the 14 peptide sequences with CAMPr3 where 16 motifs exhibited an antibacterial activity > 0.9 with iAMPpred server. Out of the 16 peptides, two had the desirable hydrophobicity of > 40%, instability index below 40 and an Isoelectric point > 6. Their 3D structures were predicted using PRIMO server, and then docked against MmpL3 of Mycobacterium tuberculosis. Results from Hdock server showed that two Peptides had the lowest docking energies of -198.13 and -193.75 for DRN7.1.2 and DB1CT.1.5 respectively. The complexes had Confidence score of 0.7236 and 0.7058 for DRN7.1.2 and DBC1T.1.2 respectively which was above 0.7 therefore the two molecules forming the complexes are more likely to bind together that is the motifs and the receptor MmpL3.Thus, finding from this study supports further exploration of AMPs as alternative treatment for Tuberculosis. | en_US |
