Nowadays antimicrobial peptides have attracted more attention as potential antimicrobial agents. Therefore, in order to investigate the thermal stability of Enterocin P peptide (EntP), the third structure of EntP was first predicted using the I-TASSER server. Then, the stability of this structure was evaluated by dynamic conditions for this purpose, the simulation was performed using GROMACS software in 400ns at cow body temperature (312° K). Finally, the root-mean-square deviation (RMSD)graph of this peptide was plotted against time along the simulation trajectory. ClusPro online server was used to study the interaction of peptide with LptD surface protein from Escherichia coli bacterium causing mastitis. In the in vitro phase of this study, the minimum inhibitory concentration (MIC) and minimum dissociation concentration (MBC) of EntP peptide were estimated based on the microbroth method on Escherichia coli. The results showed that the best predicted structure of EntP peptide by I-TASSER server had a C-score of 1.4 which was selected. The RMSD graph related to the thermal stability of EntP at bovine body temperature showed that the structure of EntP peptide is stable after 400 ns of the simulation trajectory. The results of molecular docking also showed that this peptide was correctly attached to the LptD antigen. After measuring the MIC, the bacteria were cultured and the MBC was obtained, which were estimated at 48.25 and 96.5 (μg/ml), respectively. This peptide could be used as an alternative to antibiotics or in combination with them for the treatment of infections with the origin of Escherichia coli.

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