Multidrug resistance of pathogenic microorganisms is a common problem in the treatment of infections. Therefore, searching for new agents with antimicrobial activities appears to be essential. Thrombocidin-1 (TC-1) is an antimicrobial peptide (AMP) derived from platelets. The present study aimed to produce recombinant TC-1 (rTC-1) with His tag to evaluate its antimicrobial activity and also predict its thermal-stability through molecular dynamic (MD) simulations. Minimum inhibitory concentration (MIC) and minimum bactericidal concentration of rTC-1 against bacterial isolates were determined. Considering the importance of thermal-stability of proteins in their therapeutic applications, thermal-stability of rTC-1 predicted through MD simulation during 25ns at two important temperatures including avian normal body temperature and water boiling temperature at sea level. MIC results revealed that rTC1 had the most and least potency against Salmonella enteritidis and Escherichia coli, respectively. The root-mean-square deviation of rTC-1 during 25ns MD simulations revealed that this protein is stable at avian normal body temperature (40°C) but might lose stability at water boiling temperature at sea level. rTC-1 as an AMP has a good potency against some bacterial pathogens especially Salmonella spp. and E. coli 0157:H7. rTC-1 can be used as an alternative for common antimicrobial agents used in clinical settings.
Keywords: antimicrobial peptide; recombinant thrombocidin-1; thermal-stability.