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Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide

Amphibian skin secretions are an important treasure house of bioactive antimicrobial peptides (AMPs). Despite having been the focus of decades of research in this context, investigations of phyllomedusine frogs continue to identify new AMPs from their skin secretions. In this study, the prototype of...

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Autores principales: Wu, Di, Gao, Yitian, Tan, Yining, Liu, Yuzhang, Wang, Lei, Zhou, Mei, Xi, Xinping, Ma, Chengbang, Bininda-Emonds, Olaf R. P., Chen, Tianbao, Shaw, Chris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5876494/
https://www.ncbi.nlm.nih.gov/pubmed/29628917
http://dx.doi.org/10.3389/fmicb.2018.00541
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author Wu, Di
Gao, Yitian
Tan, Yining
Liu, Yuzhang
Wang, Lei
Zhou, Mei
Xi, Xinping
Ma, Chengbang
Bininda-Emonds, Olaf R. P.
Chen, Tianbao
Shaw, Chris
author_facet Wu, Di
Gao, Yitian
Tan, Yining
Liu, Yuzhang
Wang, Lei
Zhou, Mei
Xi, Xinping
Ma, Chengbang
Bininda-Emonds, Olaf R. P.
Chen, Tianbao
Shaw, Chris
author_sort Wu, Di
collection PubMed
description Amphibian skin secretions are an important treasure house of bioactive antimicrobial peptides (AMPs). Despite having been the focus of decades of research in this context, investigations of phyllomedusine frogs continue to identify new AMPs from their skin secretions. In this study, the prototype of a novel family of AMP distinctin-like-peptide-PH (DLP-PH) was identified from the skin secretion of the otherwise well-studied Tiger-Legged Tree Frog Phyllomedusa hypochondrialis through cloning of its precursor-encoding cDNA from a skin secretion-derived cDNA library by a 3′-rapid amplification of cDNA ends (RACE) strategy. Subsequently, the mature peptide was isolated and characterized using reverse-phase HPLC and MS/MS fragmentation sequencing. DLP-PH adopted an α-helical conformation in membrane mimetic solution and demonstrated unique structural features with two distinct domains that differed markedly in their physiochemical properties. Chemically synthesized replicates of DLP-PH showed antimicrobial activity against planktonic bacterial and yeast cells, but more potent against Escherichia coli at 32 μg/mL. However, DLP-PH showed much weaker inhibitory activity against the growth of sessile cells in biofilms. In addition, DLP-PH exhibited anti-proliferative activity against human cancer cell lines, H157, and PC3, but with no major toxicity against normal human cell, HMEC-1. These combined properties make DLP-PH deserving further study as an antimicrobial agent and further investigations of its structure-activity relationship could provide valuable new insights into drug lead candidates for antimicrobial and/or anti-cancer purposes.
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spelling pubmed-58764942018-04-06 Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide Wu, Di Gao, Yitian Tan, Yining Liu, Yuzhang Wang, Lei Zhou, Mei Xi, Xinping Ma, Chengbang Bininda-Emonds, Olaf R. P. Chen, Tianbao Shaw, Chris Front Microbiol Microbiology Amphibian skin secretions are an important treasure house of bioactive antimicrobial peptides (AMPs). Despite having been the focus of decades of research in this context, investigations of phyllomedusine frogs continue to identify new AMPs from their skin secretions. In this study, the prototype of a novel family of AMP distinctin-like-peptide-PH (DLP-PH) was identified from the skin secretion of the otherwise well-studied Tiger-Legged Tree Frog Phyllomedusa hypochondrialis through cloning of its precursor-encoding cDNA from a skin secretion-derived cDNA library by a 3′-rapid amplification of cDNA ends (RACE) strategy. Subsequently, the mature peptide was isolated and characterized using reverse-phase HPLC and MS/MS fragmentation sequencing. DLP-PH adopted an α-helical conformation in membrane mimetic solution and demonstrated unique structural features with two distinct domains that differed markedly in their physiochemical properties. Chemically synthesized replicates of DLP-PH showed antimicrobial activity against planktonic bacterial and yeast cells, but more potent against Escherichia coli at 32 μg/mL. However, DLP-PH showed much weaker inhibitory activity against the growth of sessile cells in biofilms. In addition, DLP-PH exhibited anti-proliferative activity against human cancer cell lines, H157, and PC3, but with no major toxicity against normal human cell, HMEC-1. These combined properties make DLP-PH deserving further study as an antimicrobial agent and further investigations of its structure-activity relationship could provide valuable new insights into drug lead candidates for antimicrobial and/or anti-cancer purposes. Frontiers Media S.A. 2018-03-23 /pmc/articles/PMC5876494/ /pubmed/29628917 http://dx.doi.org/10.3389/fmicb.2018.00541 Text en Copyright © 2018 Wu, Gao, Tan, Liu, Wang, Zhou, Xi, Ma, Bininda-Emonds, Chen and Shaw. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Wu, Di
Gao, Yitian
Tan, Yining
Liu, Yuzhang
Wang, Lei
Zhou, Mei
Xi, Xinping
Ma, Chengbang
Bininda-Emonds, Olaf R. P.
Chen, Tianbao
Shaw, Chris
Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title_full Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title_fullStr Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title_full_unstemmed Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title_short Discovery of Distinctin-Like-Peptide-PH (DLP-PH) From the Skin Secretion of Phyllomedusa hypochondrialis, a Prototype of a Novel Family of Antimicrobial Peptide
title_sort discovery of distinctin-like-peptide-ph (dlp-ph) from the skin secretion of phyllomedusa hypochondrialis, a prototype of a novel family of antimicrobial peptide
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5876494/
https://www.ncbi.nlm.nih.gov/pubmed/29628917
http://dx.doi.org/10.3389/fmicb.2018.00541
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