3) Most AMPs are an amphipathic and this property is a key role

3). Most AMPs are an amphipathic and this property is a key role in antimicrobial activity by microbial

membrane interaction. In fact, it was previously demonstrated that the pleurocidin had a α-helical structure in the membrane-mimetic condition [36]. Similarly, NMR structural studies that covered all of the Plc-2 peptide sequence showed that in an aqueous solution the Plc presents a random coil conformation [37]. However, it assumed an α-helical structure in TFE and in dodecylphosphocholine (DPC) micelles [22]. Thus, the Plc-2 α-helical structure described in this work is similar to that for many other AMPs, which cause lysis and release of intracellular contents by binding to the surface of bacterial membranes. this website The α-helical structure produces a significant destabilizing effect upon membranes, which insert themselves into the membrane by binding more efficiently than other structural configurations [19]. This conclusion is also in agreement with a report from Yamada and Natori [41], in which the fragment corresponding to the α-helical region of sapecin B, a derived peptide belonging to the insect defensin

family, showed broad antibacterial activity. However, antimicrobial activity is not restricted exclusively to α-helical structures. Lee et al. [27] attributed the activity of the AMP tenecin to a fragment (amino acids 29–43) located in a β-sheet region of the peptide. Similarly other authors founded that the antimicrobial activity of some peptides was establish in amphipathic beta-sheet segments BMS-354825 [19]. Microbial cell surfaces such as membranes or cell wall are composed of various components, and they exhibited significant differences in surface components between bacteria and fungi. Therefore, it may be possible the membrane composition influences the activity of an AMP by influencing preferential interactions with α-helical or β-sheet (-)-p-Bromotetramisole Oxalate structures. Some known AMP can

induce abnormal morphological changes in the hyphae structure of phytopathogenic fungi [3] and human pathogenic fungi [20]. In our study, we chose to examine two fungi examined Alternaria sp. and F. oxysporum that are of economical importance. The abnormal morphological changes in membrane structure of hyphae were evaluated in vivo with the fluorescent membrane probe SG. This probe was used to assess cell permeation of fungi treated with both peptides. All the fungi showed identical fluorescent staining. Cellular membranes were compromised and also disrupted if the fungal structures were incubated with pleurocidin or Plc-2. The MIC and MFC values measured illustrate the relative antifungal potency of the two peptides with MIC values quite comparable to the conventional fungicide captan. The highest inhibitory activity of the two peptides was observed against Colletotrichum sp., and the lowest inhibition was noted against A. ochraceus ( Table 2).

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