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Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities
BACKGROUND: Antimicrobial peptides (AMPs) from the skin secretions of amphibians are now considered as a potential alternative to conventional antibiotics. Phylloseptins are a family of AMPs identified in the skin secretions of Phyllomedusinae tree frogs which exhibit highly conserved structural cha...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Dove Medical Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6350648/ https://www.ncbi.nlm.nih.gov/pubmed/30774309 http://dx.doi.org/10.2147/DDDT.S191072 |
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author | Liu, Yuzhang Du, Qiang Ma, Chengbang Xi, Xinping Wang, Lei Zhou, Mei Burrows, James F Chen, Tianbao Wang, Hui |
author_facet | Liu, Yuzhang Du, Qiang Ma, Chengbang Xi, Xinping Wang, Lei Zhou, Mei Burrows, James F Chen, Tianbao Wang, Hui |
author_sort | Liu, Yuzhang |
collection | PubMed |
description | BACKGROUND: Antimicrobial peptides (AMPs) from the skin secretions of amphibians are now considered as a potential alternative to conventional antibiotics. Phylloseptins are a family of AMPs identified in the skin secretions of Phyllomedusinae tree frogs which exhibit highly conserved structural characteristics. This study examines the structure–activity relationship of the newly discovered phylloseptin, Phylloseptin-PHa (PSPHa) from Pithecopus hypochondrialis. MATERIALS AND METHODS: PSPHa and modified analogs were produced by solid phase synthesis and purified by reverse-phase HPLC. Rationally designed modified analogs incorporating changes in significant physicochemical parameters such as hydrophobicity, hydrophobic moment and net charge were investigated to determine their influence on secondary structure, antimicrobial activity, membrane permeabilization and cytotoxicity. RESULTS: Overall, we found that when rationally designing AMPs by altering their primary structure it is important to keep a balance between hydrophobicity and charge. CONCLUSION: This study provides new insights which will help in the future development of AMPs as alternatives to conventional antibiotics for the treatment of Staphylococcus aureus and methicillin-resistant S. aureus infections. |
format | Online Article Text |
id | pubmed-6350648 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-63506482019-02-15 Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities Liu, Yuzhang Du, Qiang Ma, Chengbang Xi, Xinping Wang, Lei Zhou, Mei Burrows, James F Chen, Tianbao Wang, Hui Drug Des Devel Ther Original Research BACKGROUND: Antimicrobial peptides (AMPs) from the skin secretions of amphibians are now considered as a potential alternative to conventional antibiotics. Phylloseptins are a family of AMPs identified in the skin secretions of Phyllomedusinae tree frogs which exhibit highly conserved structural characteristics. This study examines the structure–activity relationship of the newly discovered phylloseptin, Phylloseptin-PHa (PSPHa) from Pithecopus hypochondrialis. MATERIALS AND METHODS: PSPHa and modified analogs were produced by solid phase synthesis and purified by reverse-phase HPLC. Rationally designed modified analogs incorporating changes in significant physicochemical parameters such as hydrophobicity, hydrophobic moment and net charge were investigated to determine their influence on secondary structure, antimicrobial activity, membrane permeabilization and cytotoxicity. RESULTS: Overall, we found that when rationally designing AMPs by altering their primary structure it is important to keep a balance between hydrophobicity and charge. CONCLUSION: This study provides new insights which will help in the future development of AMPs as alternatives to conventional antibiotics for the treatment of Staphylococcus aureus and methicillin-resistant S. aureus infections. Dove Medical Press 2019-01-23 /pmc/articles/PMC6350648/ /pubmed/30774309 http://dx.doi.org/10.2147/DDDT.S191072 Text en © 2019 Liu et al. This work is published and licensed by Dove Medical Press Limited The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. |
spellingShingle | Original Research Liu, Yuzhang Du, Qiang Ma, Chengbang Xi, Xinping Wang, Lei Zhou, Mei Burrows, James F Chen, Tianbao Wang, Hui Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title | Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title_full | Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title_fullStr | Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title_full_unstemmed | Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title_short | Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities |
title_sort | structure–activity relationship of an antimicrobial peptide, phylloseptin-pha: balance of hydrophobicity and charge determines the selectivity of bioactivities |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6350648/ https://www.ncbi.nlm.nih.gov/pubmed/30774309 http://dx.doi.org/10.2147/DDDT.S191072 |
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