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Toxins 2015, 7(12), 5182-5193; doi:10.3390/toxins7124878

Phylloseptin-PBa—A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity

1
Natural Drug Discovery Group, School of Pharmacy, Queen’s University, Belfast BT9 7BL, Northern Ireland, UK
2
College of Basic Medical Science, Zhejiang Chinese Medial University, Hangzhou 310053, China
3
Perubiotech Eirl, Santiago de Surco, Lima 33, Peru
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Stephen P. Mackessy
Received: 14 October 2015 / Revised: 9 November 2015 / Accepted: 23 November 2015 / Published: 1 December 2015
(This article belongs to the Special Issue Venomics, Venom Proteomics and Venom Transcriptomics)
View Full-Text   |   Download PDF [2195 KB, uploaded 1 December 2015]   |  

Abstract

Antimicrobial peptides from amphibian skin secretion display remarkable broad-spectrum antimicrobial activity and are thus promising for the discovery of new antibiotics. In this study, we report a novel peptide belonging to the phylloseptin family of antimicrobial peptides, from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea, which was named Phylloseptin-PBa. Degenerate primers complementary to putative signal peptide sites of frog skin peptide precursor-encoding cDNAs were designed to interrogate a skin secretion-derived cDNA library from this frog. Subsequently, the peptide was isolated and identified using reverse phase HPLC and MS/MS fragmentation. The synthetic replicate was demonstrated to have activity against S. aureus, E. coli and C. albicans at concentrations of 8, 128 and 8 mg/L, respectively. In addition, it exhibited anti-proliferative activity against the human cancer cell lines, H460, PC3 and U251MG, but was less active against a normal human cell line (HMEC). Furthermore, a haemolysis assay was performed to assess mammalian cell cytotoxicity of Phylloseptin-PBa. This peptide contained a large proportion of α-helical domain, which may explain its antimicrobial and anticancer activities. View Full-Text
Keywords: amphibian; antimicrobial; anticancer; peptides; molecular cloning; mass spectrometry amphibian; antimicrobial; anticancer; peptides; molecular cloning; mass spectrometry
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Wan, Y.; Ma, C.; Zhou, M.; Xi, X.; Li, L.; Wu, D.; Wang, L.; Lin, C.; Lopez, J.C.; Chen, T.; Shaw, C. Phylloseptin-PBa—A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity. Toxins 2015, 7, 5182-5193.

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