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Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor

The dermaseptin antimicrobial peptide family contains members of 27–34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs. By use of a degenerate primer in Rapid amplification of cDNA ends (RACE) PCR designed to a common conserved...

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Autores principales: Shi, Daning, Hou, Xiaojuan, Wang, Lei, Gao, Yitian, Wu, Di, Xi, Xinping, Zhou, Mei, Kwok, Hang Fai, Duan, Jinao, Chen, Tianbao, Shaw, Chris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4885059/
https://www.ncbi.nlm.nih.gov/pubmed/27187467
http://dx.doi.org/10.3390/toxins8050144
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author Shi, Daning
Hou, Xiaojuan
Wang, Lei
Gao, Yitian
Wu, Di
Xi, Xinping
Zhou, Mei
Kwok, Hang Fai
Duan, Jinao
Chen, Tianbao
Shaw, Chris
author_facet Shi, Daning
Hou, Xiaojuan
Wang, Lei
Gao, Yitian
Wu, Di
Xi, Xinping
Zhou, Mei
Kwok, Hang Fai
Duan, Jinao
Chen, Tianbao
Shaw, Chris
author_sort Shi, Daning
collection PubMed
description The dermaseptin antimicrobial peptide family contains members of 27–34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs. By use of a degenerate primer in Rapid amplification of cDNA ends (RACE) PCR designed to a common conserved domain within the 5′-untranslated regions of previously-characterized dermaseptin encoding cDNAs, two novel members of this peptide family, named dermaseptin-PD-1 and dermaseptin-PD-2, were identified in the skin secretion of the phyllomedusine frog, Pachymedusa dacnicolor. The primary structures of both peptides were predicted from cloned cDNAs, as well as being confirmed by mass spectral analysis of crude skin secretion fractions resulted from reversed-phase high-performance liquid chromatography. Chemically-synthesized replicates of dermaseptin-PD-1 and dermaseptin-PD-2 were investigated for antimicrobial activity using standard model microorganisms (Gram-positive bacteria, Gram-negative bacteria and a yeast) and for cytotoxicity using mammalian red blood cells. The possibility of synergistic effects between the two peptides and their anti-cancer cell proliferation activities were assessed. The peptides exhibited moderate to high inhibition against the growth of the tested microorganisms and cancer cell lines with low haemolytic activity. Synergistic interaction between the two peptides in inhibiting the proliferation of Escherichia coli and human neuronal glioblastoma cell line, U251MG was also manifested.
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spelling pubmed-48850592016-05-31 Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor Shi, Daning Hou, Xiaojuan Wang, Lei Gao, Yitian Wu, Di Xi, Xinping Zhou, Mei Kwok, Hang Fai Duan, Jinao Chen, Tianbao Shaw, Chris Toxins (Basel) Article The dermaseptin antimicrobial peptide family contains members of 27–34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs. By use of a degenerate primer in Rapid amplification of cDNA ends (RACE) PCR designed to a common conserved domain within the 5′-untranslated regions of previously-characterized dermaseptin encoding cDNAs, two novel members of this peptide family, named dermaseptin-PD-1 and dermaseptin-PD-2, were identified in the skin secretion of the phyllomedusine frog, Pachymedusa dacnicolor. The primary structures of both peptides were predicted from cloned cDNAs, as well as being confirmed by mass spectral analysis of crude skin secretion fractions resulted from reversed-phase high-performance liquid chromatography. Chemically-synthesized replicates of dermaseptin-PD-1 and dermaseptin-PD-2 were investigated for antimicrobial activity using standard model microorganisms (Gram-positive bacteria, Gram-negative bacteria and a yeast) and for cytotoxicity using mammalian red blood cells. The possibility of synergistic effects between the two peptides and their anti-cancer cell proliferation activities were assessed. The peptides exhibited moderate to high inhibition against the growth of the tested microorganisms and cancer cell lines with low haemolytic activity. Synergistic interaction between the two peptides in inhibiting the proliferation of Escherichia coli and human neuronal glioblastoma cell line, U251MG was also manifested. MDPI 2016-05-12 /pmc/articles/PMC4885059/ /pubmed/27187467 http://dx.doi.org/10.3390/toxins8050144 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Shi, Daning
Hou, Xiaojuan
Wang, Lei
Gao, Yitian
Wu, Di
Xi, Xinping
Zhou, Mei
Kwok, Hang Fai
Duan, Jinao
Chen, Tianbao
Shaw, Chris
Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title_full Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title_fullStr Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title_full_unstemmed Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title_short Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
title_sort two novel dermaseptin-like antimicrobial peptides with anticancer activities from the skin secretion of pachymedusa dacnicolor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4885059/
https://www.ncbi.nlm.nih.gov/pubmed/27187467
http://dx.doi.org/10.3390/toxins8050144
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