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Molecules 2018, 23(11), 2943;

Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides

Departamento de Química Orgánica, Facultad de Bioquímica y Cs. Biológicas (FBCB), Universidad Nacional del Litoral (UNL), Ciudad Universitaria, 3000 Santa Fe, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), 1825 Buenos Aires, Argentina
Proteomics Platform, Barcelona Science Park, Baldiri Reixac 10, 08028 Barcelona, Spain
CIBER-BBN, Networking Centre on Bioengineering, Biomaterials and Nanomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028 Barcelona, Spain;
Department of Organic Chemistry, University of Barcelona, 08028 Barcelona, Spain
School of Chemistry and Physics, University of KwaZulu-Natal, 4000 Durban, South Africa
Cátedras de Microbiología y Biotecnología, Departamento de Ingeniería en Alimentos, Facultad de Ingeniería Química, U.N.L. Santiago del Estero 2829, 3000 Santa Fe, Argentina
Cátedra de Ecotoxicología, Escuela Superior de Sanidad. FBCB, U.N.L. Ciudad Universitaria, 3000 Santa Fe, Argentina
Authors to whom correspondence should be addressed.
Received: 27 October 2018 / Revised: 6 November 2018 / Accepted: 9 November 2018 / Published: 11 November 2018
(This article belongs to the Section Natural Products Chemistry)
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Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs. View Full-Text
Keywords: peptides; frogs; synthesis; antimicrobial; peptidomics peptides; frogs; synthesis; antimicrobial; peptidomics

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Siano, A.; Humpola, M.V.; de Oliveira, E.; Albericio, F.; Simonetta, A.C.; Lajmanovich, R.; Tonarelli, G.G. Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides. Molecules 2018, 23, 2943.

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