Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions
Abstract Background The availability of antimicrobial peptides from several different natural sources has opened an avenue for the discovery of new biologically active molecules. To the best of our knowledge, only two peptides isolated from the frog Leptodactylus labyrinthicus, namely pentadactylin...
Published in: | Journal of Venomous Animals and Toxins including Tropical Diseases |
---|---|
Main Authors: | , , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
SciELO
2017
|
Subjects: | |
Online Access: | https://doi.org/10.1186/s40409-017-0094-y https://doaj.org/article/b4640ab0362a4237aa2fd403a9e1ef7e |
id |
ftdoajarticles:oai:doaj.org/article:b4640ab0362a4237aa2fd403a9e1ef7e |
---|---|
record_format |
openpolar |
spelling |
ftdoajarticles:oai:doaj.org/article:b4640ab0362a4237aa2fd403a9e1ef7e 2023-05-15T15:14:48+02:00 Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions Karla A. G. Gusmão Daniel M. dos Santos Virgílio M. Santos María Esperanza Cortés Pablo V. M. Reis Vera L. Santos Dorila Piló-Veloso Rodrigo M. Verly Maria Elena de Lima Jarbas M. Resende 2017-02-01T00:00:00Z https://doi.org/10.1186/s40409-017-0094-y https://doaj.org/article/b4640ab0362a4237aa2fd403a9e1ef7e EN eng SciELO http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100302&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/s40409-017-0094-y https://doaj.org/article/b4640ab0362a4237aa2fd403a9e1ef7e Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 0 (2017) Leptodactylus labyrinthicus Ocellatins Antimicrobial peptides Peptide membrane interactions Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2017 ftdoajarticles https://doi.org/10.1186/s40409-017-0094-y 2022-12-31T15:03:21Z Abstract Background The availability of antimicrobial peptides from several different natural sources has opened an avenue for the discovery of new biologically active molecules. To the best of our knowledge, only two peptides isolated from the frog Leptodactylus labyrinthicus, namely pentadactylin and ocellatin-F1, have shown antimicrobial activities. Therefore, in order to explore the antimicrobial potential of this species, we have investigated the biological activities and membrane interactions of three peptides isolated from the anuran skin secretion. Methods Three peptide primary structures were determined by automated Edman degradation. These sequences were prepared by solid-phase synthesis and submitted to activity assays against gram-positive and gram-negative bacteria and against two fungal strains. The hemolytic properties of the peptides were also investigated in assays with rabbit blood erythrocytes. The conformational preferences of the peptides and their membrane interactions have been investigated by circular dichroism spectroscopy and liposome dye release assays. Results The amino acid compositions of three ocellatins were determined and the sequences exhibit 100% homology for the first 22 residues (ocellatin-LB1 sequence). Ocellatin-LB2 carries an extra Asn residue and ocellatin-F1 extra Asn-Lys-Leu residues at C-terminus. Ocellatin-F1 presents a stronger antibiotic potential and a broader spectrum of activities compared to the other peptides. The membrane interactions and pore formation capacities of the peptides correlate directly with their antimicrobial activities, i.e., ocellatin-F1 > ocellatin-LB1 > ocellatin-LB2. All peptides acquire high helical contents in membrane environments. However, ocellatin-F1 shows in average stronger helical propensities. Conclusions The obtained results indicate that the three extra amino acid residues at the ocellatin-F1 C-terminus play an important role in promoting stronger peptide-membrane interactions and antimicrobial properties. The extra Asn-23 ... Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 23 1 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Leptodactylus labyrinthicus Ocellatins Antimicrobial peptides Peptide membrane interactions Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
spellingShingle |
Leptodactylus labyrinthicus Ocellatins Antimicrobial peptides Peptide membrane interactions Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 Karla A. G. Gusmão Daniel M. dos Santos Virgílio M. Santos María Esperanza Cortés Pablo V. M. Reis Vera L. Santos Dorila Piló-Veloso Rodrigo M. Verly Maria Elena de Lima Jarbas M. Resende Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
topic_facet |
Leptodactylus labyrinthicus Ocellatins Antimicrobial peptides Peptide membrane interactions Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
description |
Abstract Background The availability of antimicrobial peptides from several different natural sources has opened an avenue for the discovery of new biologically active molecules. To the best of our knowledge, only two peptides isolated from the frog Leptodactylus labyrinthicus, namely pentadactylin and ocellatin-F1, have shown antimicrobial activities. Therefore, in order to explore the antimicrobial potential of this species, we have investigated the biological activities and membrane interactions of three peptides isolated from the anuran skin secretion. Methods Three peptide primary structures were determined by automated Edman degradation. These sequences were prepared by solid-phase synthesis and submitted to activity assays against gram-positive and gram-negative bacteria and against two fungal strains. The hemolytic properties of the peptides were also investigated in assays with rabbit blood erythrocytes. The conformational preferences of the peptides and their membrane interactions have been investigated by circular dichroism spectroscopy and liposome dye release assays. Results The amino acid compositions of three ocellatins were determined and the sequences exhibit 100% homology for the first 22 residues (ocellatin-LB1 sequence). Ocellatin-LB2 carries an extra Asn residue and ocellatin-F1 extra Asn-Lys-Leu residues at C-terminus. Ocellatin-F1 presents a stronger antibiotic potential and a broader spectrum of activities compared to the other peptides. The membrane interactions and pore formation capacities of the peptides correlate directly with their antimicrobial activities, i.e., ocellatin-F1 > ocellatin-LB1 > ocellatin-LB2. All peptides acquire high helical contents in membrane environments. However, ocellatin-F1 shows in average stronger helical propensities. Conclusions The obtained results indicate that the three extra amino acid residues at the ocellatin-F1 C-terminus play an important role in promoting stronger peptide-membrane interactions and antimicrobial properties. The extra Asn-23 ... |
format |
Article in Journal/Newspaper |
author |
Karla A. G. Gusmão Daniel M. dos Santos Virgílio M. Santos María Esperanza Cortés Pablo V. M. Reis Vera L. Santos Dorila Piló-Veloso Rodrigo M. Verly Maria Elena de Lima Jarbas M. Resende |
author_facet |
Karla A. G. Gusmão Daniel M. dos Santos Virgílio M. Santos María Esperanza Cortés Pablo V. M. Reis Vera L. Santos Dorila Piló-Veloso Rodrigo M. Verly Maria Elena de Lima Jarbas M. Resende |
author_sort |
Karla A. G. Gusmão |
title |
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
title_short |
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
title_full |
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
title_fullStr |
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
title_full_unstemmed |
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions |
title_sort |
ocellatin peptides from the skin secretion of the south american frog leptodactylus labyrinthicus (leptodactylidae): characterization, antimicrobial activities and membrane interactions |
publisher |
SciELO |
publishDate |
2017 |
url |
https://doi.org/10.1186/s40409-017-0094-y https://doaj.org/article/b4640ab0362a4237aa2fd403a9e1ef7e |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 0 (2017) |
op_relation |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100302&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/s40409-017-0094-y https://doaj.org/article/b4640ab0362a4237aa2fd403a9e1ef7e |
op_doi |
https://doi.org/10.1186/s40409-017-0094-y |
container_title |
Journal of Venomous Animals and Toxins including Tropical Diseases |
container_volume |
23 |
container_issue |
1 |
_version_ |
1766345204136148992 |