oxysporum, for which the MIC and the MFC values were the same. From these studies, we conclude that both peptides exhibited fungistatic and fungicidal activity for all the ascomycete fungi tested. In order GW-572016 price to understand the correlation between antifungal activity and cell-surface accumulation, we examined the effects of the peptides on the cell. The integrity of the cell wall, cellular membrane and the nuclear membrane were compromised since nuclear staining was used as an indicator for the degree of access from membrane damage by antifungal activity. These results indicate that the antifungal effects of Plc-2 are due to the accumulation of Plc-2 within the plasma membrane through interaction between peptides

and the plasma membrane, rather than with the cell wall. Therefore, membrane damage from the membrane Palbociclib manufacturer interaction of Plc-2, is the major cause of cell death.

The results are also supported by amphipathic α-helical conformation as the structural feature of Plc-2, which is presented by Schiffer–Edmundson helical wheel modeling. Amphipathic α-helical peptides, with antibacterial activity, exhibit membrane-disrupting activity and Plc also displays α-helical structure in an aqueous solution, as well as in membrane mimetic environments [25]. Comparing the primary structure of Plc-2 with the structure of other antimicrobial peptides with similar activity (dermaseptin-1, ceratotoxin and PR39) and the results obtained in this work ( Fig. 1 and Table 2) it can be strongly suggested that the sequence GKAAL was the critical amino acid sequence for Montelukast Sodium the antimicrobial activity of the pleurocidin antimicrobial peptide. In summary, the potential of Plc-2 as a therapeutic peptide agent was investigated and the results suggested that one possible reason for it exerting a similar activity of Plc was because it appeared to maintenance of the native structure of pleurocidin. Actually, Plc-2 itself had strong antimicrobial activity with a much lower hemolytic effect in comparison with melittin and other well known antibiotics, such as ampicillin, vancomycin, cefotaxime, chloramphenicol and kanamycin (data

not shown). Thus, when the problem of the structure of Plc-2 is improved by peptide engineering, this peptide may help form a leading model for developing new and novel therapeutic agents. In this study, we investigated the antibacterial and antifungal activities to determine mechanisms of action for pleurocidin and short Plc derived peptides. Our results from anti-bacterial activity indicated that Plc-2 a C-terminal 12-amino acid fragment of pleurocidin contained the critical amino acid for the cytolytic activity. The data also showed that the strong antibacterial activity against human pathogenic Gram-positive and Gram-negative bacteria was not damaging to human erythrocytes. In addition, Plc-2 also exhibits a potent activity against fungicide-resistant pathogens.