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Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae
Insects possess biological defense systems that can effectively combat the invasion of external microorganisms and viruses, thereby supporting their survival in diverse environments. Antimicrobial peptides (AMPs) represent a fast-acting weapon against invading pathogens, including various bacterial...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Korean Society for Microbiology and Biotechnology
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728235/ https://www.ncbi.nlm.nih.gov/pubmed/32627752 http://dx.doi.org/10.4014/jmb.2003.03009 |
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author | Kim, Seong Ryul Choi, Kwang-Ho Kim, Kee-Young Kwon, Hye-Yong Park, Seung-Won |
author_facet | Kim, Seong Ryul Choi, Kwang-Ho Kim, Kee-Young Kwon, Hye-Yong Park, Seung-Won |
author_sort | Kim, Seong Ryul |
collection | PubMed |
description | Insects possess biological defense systems that can effectively combat the invasion of external microorganisms and viruses, thereby supporting their survival in diverse environments. Antimicrobial peptides (AMPs) represent a fast-acting weapon against invading pathogens, including various bacterial or fungal strains. A 37-residue antimicrobial peptide, papiliocin, derived from the swallowtail butterfly Papilio xuthus larvae, showed significant antimicrobial activities against several human pathogenic bacterial and fungal strains. Jelleines, isolated as novel antibacterial peptides from the Royal Jelly (RJ) of bees, exhibit broad-spectrum protection against microbial infections. In this study, we developed a novel antimicrobial peptide, PAJE (RWKIFKKPFKISIHL-NH(2)), which is a hybrid peptide prepared by combining 1–7 amino acid residues (RWKIFKK-NH(2)) of papiliocin and 1–8 amino acid residues (PFKISIHL-NH(2)) of Jelleine-1 to alter length, charge distribution, net charge, volume, amphipaticity, and improve bacterial membrane interactions. This novel peptide exhibited increased hydrophobicity and net positive charge for binding effectively to the negatively charged membrane. PAJE demonstrated antimicrobial activity against both gram-negative and gram-positive bacteria, with very low toxicity to eukaryotic cells and an inexpensive process of synthesis. Collectively, these findings suggest that this novel peptide possesses great potential as an antimicrobial agent. |
format | Online Article Text |
id | pubmed-9728235 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Korean Society for Microbiology and Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-97282352022-12-13 Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae Kim, Seong Ryul Choi, Kwang-Ho Kim, Kee-Young Kwon, Hye-Yong Park, Seung-Won J Microbiol Biotechnol Research article Insects possess biological defense systems that can effectively combat the invasion of external microorganisms and viruses, thereby supporting their survival in diverse environments. Antimicrobial peptides (AMPs) represent a fast-acting weapon against invading pathogens, including various bacterial or fungal strains. A 37-residue antimicrobial peptide, papiliocin, derived from the swallowtail butterfly Papilio xuthus larvae, showed significant antimicrobial activities against several human pathogenic bacterial and fungal strains. Jelleines, isolated as novel antibacterial peptides from the Royal Jelly (RJ) of bees, exhibit broad-spectrum protection against microbial infections. In this study, we developed a novel antimicrobial peptide, PAJE (RWKIFKKPFKISIHL-NH(2)), which is a hybrid peptide prepared by combining 1–7 amino acid residues (RWKIFKK-NH(2)) of papiliocin and 1–8 amino acid residues (PFKISIHL-NH(2)) of Jelleine-1 to alter length, charge distribution, net charge, volume, amphipaticity, and improve bacterial membrane interactions. This novel peptide exhibited increased hydrophobicity and net positive charge for binding effectively to the negatively charged membrane. PAJE demonstrated antimicrobial activity against both gram-negative and gram-positive bacteria, with very low toxicity to eukaryotic cells and an inexpensive process of synthesis. Collectively, these findings suggest that this novel peptide possesses great potential as an antimicrobial agent. The Korean Society for Microbiology and Biotechnology 2020-09-28 2020-07-15 /pmc/articles/PMC9728235/ /pubmed/32627752 http://dx.doi.org/10.4014/jmb.2003.03009 Text en Copyright © 2020 The Korean Society for Microbiology and Biotechnology https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research article Kim, Seong Ryul Choi, Kwang-Ho Kim, Kee-Young Kwon, Hye-Yong Park, Seung-Won Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title | Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title_full | Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title_fullStr | Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title_full_unstemmed | Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title_short | Development of a Novel Short Synthetic Antibacterial Peptide Derived from the Swallowtail Butterfly Papilio xuthus Larvae |
title_sort | development of a novel short synthetic antibacterial peptide derived from the swallowtail butterfly papilio xuthus larvae |
topic | Research article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728235/ https://www.ncbi.nlm.nih.gov/pubmed/32627752 http://dx.doi.org/10.4014/jmb.2003.03009 |
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