ABSTRACT Preprodermaseptins are a rapidly expanding family of peptide precursors identified in frog skin, with conserved preproregions and markedly diverse C-terminal domains giving rise to mature antimicrobial peptides with very different lengths, sequences and conformations. Fifty different antimicrobial peptides, 10-46 residues in length, have been characterized in evolutionary distant frog species and grouped to form 7 distinct subfamilies. They include dermaseptins and phylloxins, linear and amphipathic α-helical peptides, brevinins and esculentins, loop-forming peptides with a disulfide bridge at the C-terminus, and temporins, small-sized hydrophobic peptides, 10-13 residue long. Most of these peptides are cidal against a broad spectrum of microorganisms but have no or little harmful effect on human cells. Their microbicidal effect very likely results from their capacity to permeate or disrupt the target cells. This make them promising candidates for inclusion in new treatments of nosocomial infections and multidrug-resistant infections.
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