Abstract
Glutathione s-transferases(GSTs) are enzymes involved in the conjugation and deactivation of various xenobiotics including drugs. Thisin-silico study was undertaken in order to investigate the interaction between beta-class glutathione s-transferase and five selected antibiotics, namely; ampicillin, tetracycline, chloramphenicol, ciprofloxacin and cephalexin using molecular docking study. RaptorX server was used to predict the amino acids involved at the binding sitewhile molecular docking study was employed in order to investigate the binding interactions.RaptorX predicted several amino acids which were different from the ones observed in molecular docking because of the variability in the substrate binding site of GSTs however, all the amino acids predicted by RaptorX were also found to be involved in the GSH binding.Lys107, Phe109, Ser110, Leu113, Trp114, His115 and Arg123, Leu168 were the amino acids involved in the binding of various antibiotics to the substrate binding site of the protein while Ala9, Cys10, Leu32, Tyr51, Val52, Pro53, Glu65 and Ala66were involved in the binding of the co-substrate GSH to the binding site of the protein. The results indicated that all the antibiotics showed a good binding affinity with the beta class GST and are therefore capable of deactivating the drugs. With these, finding a beta class GST inhibitors alongside antibiotics during a treatment of diseases will be of beneficial in the current fight against antibiotic resistance.
Highlights
Glutathione s-transferases(GSTs) are enzymes involved in the conjugation and deactivation of various xenobiotics including drugs
GSTs contained two binding sites with different amino acids participating in the interaction of ligands to these binding sites
Comparative analysis between the predicted binding pocket amino acids and sequence alignment study showed that C10, V52, P53, H106, K107 and W164 were all perfectly conserved in all the beta class GSTs analyzed (Fig 1)
Summary
Glutathione s-transferases(GSTs) are enzymes involved in the conjugation and deactivation of various xenobiotics including drugs. While the enzyme is beneficial in the detoxification of several toxins that can be harmful to living organisms at the same time, the detoxification of several drugs which in other ways serve to save the lives of the organism is threatening the existence of human race as a whole (Arca et al, 1988; Morrow et al, 1998) This prompted a lot of researches on inhibitors of GST especially during treatment of certain diseases such as cancer(Allocati et al, 2018).Several different isoenzymes of GST have been identified in bacteria including Beta, Chi, Zeta, Rho, Nu, and Theta classes(Shehu et al, 2019). Used to investigate the interaction between beta-class glutathione –transferase and five selected antibiotics, namely; ampicillin, tetracycline, chloramphenicol, ciprofloxacin and cephalexin using molecular docking study
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