Next Article in Journal
Clinical Significance of Carbapenem-Tolerant Pseudomonas aeruginosa Isolated in the Respiratory Tract
Next Article in Special Issue
Caerin 1 Antimicrobial Peptides that Inhibit HIV and Neisseria May Spare Protective Lactobacilli
Previous Article in Journal
Prevalence and Antibiotic Resistance of ESKAPE Pathogens Isolated in the Emergency Department of a Tertiary Care Teaching Hospital in Hungary: A 5-Year Retrospective Survey
Previous Article in Special Issue
Activity of Temporin A and Short Lipopeptides Combined with Gentamicin against Biofilm Formed by Staphylococcus aureus and Pseudomonas aeruginosa
Open AccessArticle

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

1
Laboratory of Toxinology, Department of Physiological Sciences, Institute of Biology, University of Brasília, Brasília 70.910-900, DF, Brazil
2
Laboratory of Protein Chemistry and Biochemistry, Department of Cell Biology, Institute of Biology, University of Brasília, Brasília 70.910-900, DF, Brazil
3
Laboratory of Gene Biology, Department of Cell Biology, Institute of Biology, University of Brasília, Brasília 70.910-900, DF, Brazil
4
Laboratory of Biophysics, Department of Cell Biology, Institute of Biology, University of Brasília, Brasília 70.910-900, DF, Brazil
*
Author to whom correspondence should be addressed.
Antibiotics 2020, 9(9), 625; https://doi.org/10.3390/antibiotics9090625
Received: 1 July 2020 / Revised: 17 August 2020 / Accepted: 19 August 2020 / Published: 21 September 2020
(This article belongs to the Special Issue Development of Antimicrobial Peptides from Amphibian)
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. View Full-Text
Keywords: amphibian; Boana raniceps; skin secretion; structural analysis; antimicrobial peptide; cytolytic peptide; hemolysis amphibian; Boana raniceps; skin secretion; structural analysis; antimicrobial peptide; cytolytic peptide; hemolysis
Show Figures

Figure 1

MDPI and ACS Style

Santana, C.J.C.; Magalhães, A.C.M.; dos Santos Júnior, A.C.M.; Ricart, C.A.O.; Lima, B.D.; Álvares, A.C.M.; Freitas, S.M.; Pires, O.R., Jr.; Fontes, W.; Castro, M.S. Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties. Antibiotics 2020, 9, 625.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop