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Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions

Overview of attention for article published in Journal of Venomous Animals and Toxins including Tropical Diseases, January 2017
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Title
Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases, January 2017
DOI 10.1186/s40409-017-0094-y
Pubmed ID
Authors

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

Abstract

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. 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. 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. 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 residue present in ocellatin-LB2 sequence seems to decrease its antimicrobial potential and the strength of the peptide-membrane interactions.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 46 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 46 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 12 26%
Student > Master 7 15%
Student > Ph. D. Student 6 13%
Researcher 3 7%
Professor > Associate Professor 3 7%
Other 4 9%
Unknown 11 24%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 10 22%
Agricultural and Biological Sciences 7 15%
Chemistry 7 15%
Pharmacology, Toxicology and Pharmaceutical Science 2 4%
Environmental Science 1 2%
Other 4 9%
Unknown 15 33%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 24 January 2017.
All research outputs
#15,517,992
of 25,374,647 outputs
Outputs from Journal of Venomous Animals and Toxins including Tropical Diseases
#260
of 539 outputs
Outputs of similar age
#230,206
of 420,482 outputs
Outputs of similar age from Journal of Venomous Animals and Toxins including Tropical Diseases
#6
of 11 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 37th percentile – i.e., 37% of other outputs scored the same or lower than it.
So far Altmetric has tracked 539 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.6. This one is in the 49th percentile – i.e., 49% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 420,482 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 44th percentile – i.e., 44% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 11 others from the same source and published within six weeks on either side of this one. This one is in the 45th percentile – i.e., 45% of its contemporaries scored the same or lower than it.