Enzymatic Inhibition of Phytochemical from Garcinia imberti on Homology Modelled Beta-lactamase Protein in Staphylococcus sciuri

Objectives: To analyze the interactions of modeled Beta-lactamase from Staphylococcus sciuri with phytochemical compounds from medicinal plant, Garcinia imberti in the docked complex. Methods: The protein-protein blast (BLASTP) analysis of target sequence of Beta-lactamase protein from Staphylococcus sciuri, against protein data bank (PDB) resulted that the X-ray crystal structure of beta-lactamase from Staphylococcus aureus was carried out. The sequence alignment was performed to build the initial model of Beta-lactamase protein from Staphylococcus sciuri using Modeler 9v9 by applying spatial restraints from the initial structure, a bundle of 3 models were developed using random generation for further analysis. The Ramachandran plot of the energy minimized model of Beta-lactamase protein from Staphylococcus sciuri was also carried out. The modeled Betalactamase protein from S. sciurii was subjected to difference of Gaussian (DoG) site scorer to predict the possible binding sites. Results: The results indicate that 4-Butylanisole and trans-9-Octadecene exhibited promising inhibitory activity. The docking studies also implies that the conserved amino acids Glutamine and Asparagine, Lysine and Phenyl alanine in the active site of beta-lactamase are critical in binding compounds with these receptor. These docking interactions implies that the =O (keto group) present in the compounds and NH (amino group) on the amino acids favors the H bond interactions. Conclusion: The present findings throws light for the design of novel beta lactamase inhibitor compounds with antimicrobial activity envisages that the amino acids Glutamine (Q) and Asparagine (N), Lysine (L) and Phenyl alanine (F) should be considered during its design for implying its action as a best antimicrobial compound to target S. sciurii.