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. 2020 Sep 21;9(9):625.
doi: 10.3390/antibiotics9090625.

Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties

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Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties

Carlos José Correia Santana et al. Antibiotics (Basel). .

Abstract

Amphibian skin secretions are abundant in bioactive compounds, especially antimicrobial peptides. These molecules are generally cationic and rich in hydrophobic amino acids, have an amphipathic structure and adopt an α-helical conformation when in contact with microorganisms membranes. In this work, we purified and characterized Figainin 1, a novel antimicrobial and antiproliferative peptide from the cutaneous secretion of the frog Boana raniceps. Figainin 1 is a cationic peptide with eighteen amino acid residues-rich in leucine and isoleucine, with an amidated C-terminus-and adopts an α-helical conformation in the presence of trifluoroethanol (TFE). It displayed activity against Gram-negative and especially Gram-positive bacteria, with MIC values ranging from 2 to 16 µM, and showed an IC50 value of 15.9 µM against epimastigote forms of T. cruzi; however, Figanin 1 did not show activity against Candida species. This peptide also showed cytolytic effects against human erythrocytes with an HC50 of 10 µM, in addition to antiproliferative activity against cancer cells and murine fibroblasts, with IC50 values ranging from 10.5 to 13.7 µM. Despite its adverse effects on noncancerous cells, Figainin 1 exhibits interesting properties for the development of new anticancer agents and anti-infective drugs against pathogenic microorganisms.

Keywords: Boana raniceps; amphibian; antimicrobial peptide; cytolytic peptide; hemolysis; skin secretion; structural analysis.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
(A) Reversed-phase HPLC profile of B. raniceps skin secretion fractionated on a Vydac C8 column. One antibacterial fraction is indicated as Br24. The blue line shows the concentration of solution B (acetonitrile + TFA 0.1%, v/v). (B) Purification of the antimicrobial peptide (present in Br24 fraction) on a Shim-pack VP-ODS C18 column.
Figure 2
Figure 2
MALDI-TOF mass spectrum of the antibacterial peptide (isolated from Br24 fraction). In the insert is shown the presence of sodium (+22 Da) and potassium (+38 Da) adducts.
Figure 3
Figure 3
(A) Sequence alignment of the antibacterial peptide (isolated from Br24 fraction) with other putative antimicrobial peptides from B. raniceps [25] leading to the identification of Figainin 1, and (B) sequence alignment of Figainin 1 with Hylins (antimicrobial peptides isolated from other species in Boana genus). Differences of amino acids are highlighted in gray, ‘*’ indicates identical amino acids and ‘:’ indicates conservative substitutions.
Figure 4
Figure 4
(A) Circular dichroism spectra of Figainin 1 dissolved in water and in crescent concentrations (10, 30 and 50%, v/v) of trifluoroethanol (TFE). (B) Helical wheel representation of Figainin 1 illustrating the amphipathic character of the putative α-helix.
Figure 5
Figure 5
The hemolytic effect of Figainin 1 on human erythrocytes (hRBCs).
Figure 6
Figure 6
The effect of Figainin 1 on the proliferation of (A) murine skin melanoma B16F10 cells, (B) human mammary adenocarcinoma MCF-7 cells and (C) human cervical adenocarcinoma HeLa cells.

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