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In order to expand knowledge of the mechanism of action of hRNases against C. albicans, which was observed to take place by a dual mode [21], we aimed here to characterize the antifungal properties of the hRNase derived N-terminal peptides. This comparative study of the N-terminal region of the eight human hRNases against an eukaryotic pathogen such as C. albicans, has allowed us to deepen in the mechanism of action of these proteins. The present results corroborate that the antimicrobial activity of hRNases against fungi is also preserved at their N-terminal domain. The data reveal a high antifungal activity, with MFC values at sub micromolar range for most tested derivative peptides, being the RNase N-terminal derived peptides 3, 6 and 7 the most effective ones (Table 2). These results are in agreement with previous studies where the parental proteins were tested against C. albicans [21] and the derivative peptides assayed against different Gram-negative/Gram-positive bacterial species [23,24,32,57]. In addition, the current data using C. albicans reinforce the correlation between the peptide antimicrobial mechanism of action and the respective depolarization and membrane permeabilization activities displayed by the eight parental RNase peptides, in agreement with previous results [23].
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