In silico Molecular docking of lead nitrate interaction with replication compounds of E. coli

Backgrounds: According to studies, Lead is a major used extensively in industry. Native lead israre in nature. Currently lead is usually found in with nitrate or others salt lead no fundamentalfunction in the human body. Most heavy metals can be soluble in water and this is a big threat.Lead nitrate is toxic to human and it has large impact on protein metabolism and the geneticsystem. Escherichia coli is a Gram-negative, facultative anaerobic bacterium. DNA replication isa biological phenomenon. It requires a complex of enzymes and proteins to occur. Bacterialreplication enzymes have vital functions, disruption of each of which can cause serious damageto the bacterial genome.Materials and Methods: At the first the amino acid sequences of some of replication enzymesand proteins are obtained from National Center for Biotechnology Information (NCBI) ProteinDatabase. The lead Nitrate molecular formula is provided from PubChem and the crystalstructure containing the lead heavy metal was designed by chemical engineering software then soas to carry out energy minimization, it transferred into Hyperchem software. In order toinvestigate the mode of the lead with enzyme active site docking study was performed byMolegro Virtual Docking software.Results: Docking data revealed the hydrogen bond and hydrophobic interactions were involvedin the lead-receptor interactions.Conclusion: Our results revealed the possible attachment sites of lead ions and their interactionswith domains that have metal bonding properties.

کلیدواژه ها:

Heavy metal ، Simulations ، Molecular dynamics ، Docking ، Lead