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Online Journal of Bioinformatics ©
Volume 18(1):30-38, 2017
In silico docking of hydrazone derivatives with Sortase A from Staphylococcus aureus.
V Laxmi Prasanna1, R Narender.2
1Asst. Prof Chemistry Vignan institute of technology and science Deshmukhi, 2Professor Chemistry, CMR College of Engineering & Technology, Kandlakoya, Hyderabad, India.
Prasanna VL, Narender R., In silico docking hydrazone derivative with Sortase A from Staphylococcus aureus, Onl J Bioinform., 18(1):30-38, 2017. Sortase A (from Staphylococcus aureus) model was built by homology-modeling with the MODELLER program. The 3-D structure of Sortase A from Staphylococcus aureus was used as a target to determine binding, inhibitor binding position and affinities using GOLD software scoring fitness functions. Structures of synthesized compounds were confirmed by 1H NMR and Mass spectral data. Synthesized hydrazone derivative 4a-4g was a mixture of rotameric antiperiplanar and synperiplanar spectra. In silico binding to bacterial protein confirmed inhibitory activity. Amino acid residues ARG130, ASP132, SER133, VAL 134, ASP135, PHE136, GLN152 in Sortase A were involved in inhibitor recognition via hydrogen bonding interactions which stabilized target-ligand complex. The results suggest that conserved amino-acid residues in Sortase A may affect functional conformation and are directly involved in donor substrate binding.
Key words: Docking, insilico studies, Sortase A, Staphylococcus aureus.