Defense peptides are known to provide an important role in innate plant immunity to biotic environmental stress factors, including fungal diseases. Hevein-like peptides (six and ten cysteine-containing molecules) were preliminary characterized by the presence of a chitin-binding domain, which is needed to initially act on plant pathogenic filamentous fungi followed by disruption of fungal cell wall biosynthesis. Already published data indicate that these peptides can effectively inhibit non-chitin microbes, such as oomycetes. One alternative molecular mechanism of action is associated with blocking of zinc-containing metalloproteinase (fungalysin) secreted by Fusarium spp. and cleavage by plant chitinases. In our studies, we isolated and characterized two hevein-like peptides with ten-cysteine motifs each (called EAMP and LAMP), which belong to the WAMP subfamily, from barnyard grass (Echinochloa crusgalli) kernels and lyme grass (Leymus arenarius) ears, respectively. All of these molecules are homologous and contain a single amino acid substitution based on the model WAMP-1a peptide. Their recombinant analogueshave been obtained by heterologous expression in an Escherichia coli system, a spectrum of antifungal activity against some plant pathogenic and opportunistic fungal species has been determined, and it has been shown that their ability to recover total protease and chitinase activity in vitro after incubation with concentrated culture liquids of F. oxysrorum, F. solani, and F. sporotrichoides. These results suggest that these peptides can beconsidered antimicrobials and novel fungal protease inhibitors.