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Dendropsophin 1, a novel antimicrobial peptide from the skin secretion of the endemic Colombian frog Dendropsophus columbianus

In efforts to find new antimicrobial peptides (AMPs), we studied the skin secretion of the endemic Colombian frog Dendropsophus columbianus belonging to a genus that has not been investigated previously. From HPLC-fractionated secretion, we identified one peptide with slightly antibacterial activity...

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Published in:Natural product research 2018-06, Vol.32 (12), p.1383-1389
Main Authors: Triana-Vidal, Luz Elena, Castro, Mariana Souza, Pires Júnior, Osmindo Rodrigues, Álvares, Alice Cunha Morales, de Freitas, Sonia Maria, Fontes, Wagner, Vargas, Jimmy Alexander Guerrero, Zúñiga-Baos, Jorge Alberto, Correia Batista, Isabel de Fátima, Grellier, Philippe, Charneau, Sébastien
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creator Triana-Vidal, Luz Elena
Castro, Mariana Souza
Pires Júnior, Osmindo Rodrigues
Álvares, Alice Cunha Morales
de Freitas, Sonia Maria
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Vargas, Jimmy Alexander Guerrero
Zúñiga-Baos, Jorge Alberto
Correia Batista, Isabel de Fátima
Grellier, Philippe
Charneau, Sébastien
description In efforts to find new antimicrobial peptides (AMPs), we studied the skin secretion of the endemic Colombian frog Dendropsophus columbianus belonging to a genus that has not been investigated previously. From HPLC-fractionated secretion, we identified one peptide with slightly antibacterial activity. Its peptide sequence showed no sequence similarity to current annotated peptides. We named this novel peptide dendropsophin 1 (Dc1). Afterward, two analogues were designed (Dc1.1 and Dc1.2) to improve the cationic and amphipathic features. Then, their antiproliferative and cytotoxic properties were evaluated against several pathogens including bacteria, fungi, protozoa and also mammalian cells. Dc1 and its two analogues exhibited moderate antibacterial activities and no hemolytic and cytotoxic effects on mammalian cells. Analogue Dc1.2 showed slightly improved antibacterial properties. Their secondary structures were characterised using CD spectroscopy and Dc1.2 displayed a higher α-helix content and thermal stability compared to Dc1 and Dc1.1 in hydrophobic experimental conditions.
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From HPLC-fractionated secretion, we identified one peptide with slightly antibacterial activity. Its peptide sequence showed no sequence similarity to current annotated peptides. We named this novel peptide dendropsophin 1 (Dc1). Afterward, two analogues were designed (Dc1.1 and Dc1.2) to improve the cationic and amphipathic features. Then, their antiproliferative and cytotoxic properties were evaluated against several pathogens including bacteria, fungi, protozoa and also mammalian cells. Dc1 and its two analogues exhibited moderate antibacterial activities and no hemolytic and cytotoxic effects on mammalian cells. Analogue Dc1.2 showed slightly improved antibacterial properties. Their secondary structures were characterised using CD spectroscopy and Dc1.2 displayed a higher α-helix content and thermal stability compared to Dc1 and Dc1.1 in hydrophobic experimental conditions.</abstract><cop>England</cop><pub>Taylor &amp; Francis</pub><pmid>28659061</pmid><doi>10.1080/14786419.2017.1346646</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-9364-7289</orcidid><orcidid>https://orcid.org/0000-0003-4153-0465</orcidid></addata></record>
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subjects Amphibians
analogues
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Anti-Infective Agents - chemistry
Anti-Infective Agents - pharmacology
Antibacterial activity
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
antimicrobial peptide
Antimicrobial peptides
Anura
Anuran
Chemical Sciences
Colombia
Cytotoxicity
dendropsophin
Dendropsophus columbianus
Drug Evaluation, Preclinical - methods
Fungi
Hemolysis - drug effects
Hemolytic Agents - chemistry
Hemolytic Agents - pharmacology
High-performance liquid chromatography
Humans
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
Life Sciences
Liquid chromatography
Male
Mammalian cells
Mammals
Medicinal Chemistry
Microbial Sensitivity Tests
Microbiology and Parasitology
Parasitology
Peptides
Pharmaceutical sciences
Pharmacology
Protein Stability
Protein Structure, Secondary
Protozoa
Rats
Secretion
Sequence Homology, Amino Acid
Skin
Skin - secretion
Spectroscopy
Thermal stability
Trypanosoma - drug effects
title Dendropsophin 1, a novel antimicrobial peptide from the skin secretion of the endemic Colombian frog Dendropsophus columbianus
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