Introduction In recent years, a number of studies showed the biological activities of peptides derived by proteolytic cleavage of physiological proteins. These functional units, called cryptides, can be characterized by activities similar or different to those of the precursor protein. The present study was aimed to evaluate the fungicidal properties of a synthetic peptide (K13L, KKLVAASQAALGL), representing the C-terminal fragment of human albumin found in serum. Materials and Methods The synthetic peptide was obtained by solid-phase synthesis chemistry and evaluated for its biological properties by consolidated experimental methods. The in vitro fungicidal activity was investigated against different yeast species, inclusive of multidrug resistant strains. The ex vivo and in vivo anticandidal efficacy was evaluated in a model of C. albicans infection in porcine oral mucosa and in experimentally infected larvae of Galleria mellonella, respectively. Furthermore, haemolytic, cytotoxic and genotoxic properties were verified. The effect of peptide treatment on C. albicans cells was studied by confocal microscopy and transmission and scanning electron microscopy. Results K13L peptide proved to be fungicidal in vitro against the investigated yeasts at micromolar concentrations, to reduce fungal infiltration in porcine oral mucosa ex vivo, and to exert a therapeutic effect in vivo in the invertebrate animal model, without showing toxic effects on mammalian cells. Microscopic studies demonstrated that the peptide penetrates and accumulates in fungal cells causing gross morphological alterations in cellular structure. Conclusions Overall, our data prove that fragments from physiological serum proteins, as K13L peptide, may exert an antifungal activity, as previously shown for antibody-derived peptides, suggesting a potential role of these molecules in antifungal homeostasis and establishing serum proteins as a source of new antimicrobial agents.

Antifungal activity of the C-terminal peptide from human serum albumin / Ciociola, Tecla; Pier Paolo, Zanello; Conti, Stefania; Giovati, Laura; Ferrari, Elena; D'Adda, Tiziana; Magliani, Valter; Polonelli, Luciano. - STAMPA. - (2016), pp. 117-118.

Antifungal activity of the C-terminal peptide from human serum albumin

CIOCIOLA, Tecla;CONTI, Stefania;GIOVATI, Laura;FERRARI, Elena;D'ADDA, Tiziana;MAGLIANI, Valter;POLONELLI, Luciano
2016-01-01

Abstract

Introduction In recent years, a number of studies showed the biological activities of peptides derived by proteolytic cleavage of physiological proteins. These functional units, called cryptides, can be characterized by activities similar or different to those of the precursor protein. The present study was aimed to evaluate the fungicidal properties of a synthetic peptide (K13L, KKLVAASQAALGL), representing the C-terminal fragment of human albumin found in serum. Materials and Methods The synthetic peptide was obtained by solid-phase synthesis chemistry and evaluated for its biological properties by consolidated experimental methods. The in vitro fungicidal activity was investigated against different yeast species, inclusive of multidrug resistant strains. The ex vivo and in vivo anticandidal efficacy was evaluated in a model of C. albicans infection in porcine oral mucosa and in experimentally infected larvae of Galleria mellonella, respectively. Furthermore, haemolytic, cytotoxic and genotoxic properties were verified. The effect of peptide treatment on C. albicans cells was studied by confocal microscopy and transmission and scanning electron microscopy. Results K13L peptide proved to be fungicidal in vitro against the investigated yeasts at micromolar concentrations, to reduce fungal infiltration in porcine oral mucosa ex vivo, and to exert a therapeutic effect in vivo in the invertebrate animal model, without showing toxic effects on mammalian cells. Microscopic studies demonstrated that the peptide penetrates and accumulates in fungal cells causing gross morphological alterations in cellular structure. Conclusions Overall, our data prove that fragments from physiological serum proteins, as K13L peptide, may exert an antifungal activity, as previously shown for antibody-derived peptides, suggesting a potential role of these molecules in antifungal homeostasis and establishing serum proteins as a source of new antimicrobial agents.
Antifungal activity of the C-terminal peptide from human serum albumin / Ciociola, Tecla; Pier Paolo, Zanello; Conti, Stefania; Giovati, Laura; Ferrari, Elena; D'Adda, Tiziana; Magliani, Valter; Polonelli, Luciano. - STAMPA. - (2016), pp. 117-118.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/2820181
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