The Skin Secretion of the Amphibian Phyllomedusa nordestina: A Source of Antimicrobial and Antiprotozoal Peptides

Abstract

Antimicrobial peptides (AMPs) from the dermaseptin and phylloseptin families were isolated from the skin secretion of Phyllomedusa nordestina, a recently described amphibian species from Northeastern Brazil. One dermaseptin and three phylloseptins were chosen for solid phase peptide synthesis. The antiprotozoal and antimicrobial activities of the synthetic peptides were determined, as well as their cytotoxicity in mouse peritoneal cells. AMPs are being considered as frameworks for the development of novel drugs inspired by their mechanism of action.

Structure and function of a novel antioxidant peptide from the skin of tropical frogs

“…Even though the arsenal of bioactive peptides in the skin of each amphibian species is generally different, the identification of the same bioactive peptide in more than one amphibian species was previously reported. Namely, the case of the antimicrobial peptide dermaseptin 01 [48] originally identified in P. oreades, that was afterwards also identified in other three species in same genus: P. azurea, P. nordestina, and P. hypochondrialis [49,50].I n this work, we report the peptide antioxidin-I that was present in three genera of tropical amphibians. These observations evidence that antioxidin-I potentially performs an important and an efficient physiological role contributing to maintenance of frog's homeostasis.…”

“…The evaluation of the cytotoxicity of peptides isolated from amphibian skin in normal cells is relevant and important to determine the biocompatibility. Brand and co-workers [50] demonstrated that peptides isolated from the skin secretion of Phyllomedusa nordestina had no toxicity against mouse peritoneal macrophages. Additionally, low hemolytic and cytotoxic activity were detected in human erythrocytes and in the murine fibroblasts cell line NIH3T3, after 60 h exposure to peptides isolated from the skin secretion of the frog Leptodactylus pustulatus [59].…”

Dermaseptin-S1 decreasesCandida albicansgrowth, biofilm formation and the expression of hyphal wall protein 1 and aspartic protease genes

“…Similar to human skin, amphibian skin exhibits a well‐developed chemical defence system by secreting antimicrobial peptides with a wide range of pharmacological activities (Brand et al . ). These peptides are synthesized and stored in the granular glands and are released when required, usually in response to a stressor, such as a predatory attack or an infection (Amiche et al .…”

“…Dermaseptins, a large family of antimicrobial amphipathic peptides (AMP) effective against bacteria, yeasts, fungi, protozoa and viruses, are part of host defence mechanisms against pathogens . Similar to human skin, amphibian skin exhibits a well-developed chemical defence system by secreting antimicrobial peptides with a wide range of pharmacological activities (Brand et al 2013). These peptides are synthesized and stored in the granular glands and are released when required, usually in response to a stressor, such as a predatory attack or an infection (Amiche et al 2008).…”

Ocellatin‐PT antimicrobial peptides: High‐resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems

“…Regarding antiparasitic activity of AMPs, only 83 of more than 990 active peptides derived from amphibians registered at APD have been tested as antiparasitic, mostly having been tested for antimalaria activity . Furthermore, no correlation between antibacterial and antiparasitic activity potencies was observed in those AMPs that have been tested . Antimicrobial peptides have potential to form a new class of molecules able to treat neglected diseases, including those caused by parasites .…”