Publications by authors named "Arina G Arakelian"
Article Synopsis
- Endolysins from bacteriophages can break down bacterial cell walls and are used in various industries to combat biofilms and infections.
- The study focused on understanding how single-domain endolysins bind to peptidoglycan, using computational methods like molecular docking and bioinformatics, which are easier compared to experimental methods.
- The research found that Autodock Vina and the 3D-RISM module supported prior findings on the binding mechanism of a specific endolysin, showing that both computational tools effectively predicted the binding and interaction of endolysins with peptidoglycan.
Bioinformatics analysis of the sequences of orthologous zinc-containing peptidases of the M15_C subfamily revealed the presence of a conserved tryptophan residue near the active site, which is not involved in the formation of the protein core. Site-directed mutagenesis of this Trp114/109 residue using two representatives of the family, l-alanoyl-d-glutamate peptidases of bacteriophages T5 (calcium-activated EndoT5) and RB49 (EndoRB49, without ion regulation) as examples, and further analysis of the H NMR spectra of the mutants showed that a decrease in the volume of the W → F → A residue leads to changes in the hydrophobic core and active center of the protein, and also decreases the affinity for regulatory Ca in the EndoT5 mutants. The inactive T5W114A mutant lacks the ability to bind the substrate.
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