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The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide
Amphipathic α-helical antimicrobial peptides comprise a class of broad-spectrum agents that are used against pathogens. We designed a series of antimicrobial peptides, CP-P (KWKSFIKKLTSKFLHLAKKF) and its derivatives, and determined their minimum inhibitory concentrations (MICs) against Pseudomonas a...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299254/ https://www.ncbi.nlm.nih.gov/pubmed/22518150 http://dx.doi.org/10.1155/2012/764834 |
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author | Jin-Jiang, Huang Jin-Chun, Lu Min, Lu Qing-Shan, Huang Guo-Dong, Li |
author_facet | Jin-Jiang, Huang Jin-Chun, Lu Min, Lu Qing-Shan, Huang Guo-Dong, Li |
author_sort | Jin-Jiang, Huang |
collection | PubMed |
description | Amphipathic α-helical antimicrobial peptides comprise a class of broad-spectrum agents that are used against pathogens. We designed a series of antimicrobial peptides, CP-P (KWKSFIKKLTSKFLHLAKKF) and its derivatives, and determined their minimum inhibitory concentrations (MICs) against Pseudomonas aeruginosa, their minimum hemolytic concentrations (MHCs) for human erythrocytes, and the Therapeutic Index (MHC/MIC ratio). We selected the derivative peptide K11, which had the highest therapeutic index (320) among the tested peptides, to determine the MICs against Gram-positive and Gram-negative bacteria and 22 clinical isolates including Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, Pseudomonas aeruginosa, Staphylococcus epidermidis, and Klebsiella pneumonia. K11 exhibited low MICs (less than 10 μg/mL) and broad-spectrum antimicrobial activity, especially against clinically isolated drug-resistant pathogens. Therefore, these results indicate that K11 is a promising candidate antimicrobial peptide for further studies. |
format | Online Article Text |
id | pubmed-3299254 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-32992542012-04-19 The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide Jin-Jiang, Huang Jin-Chun, Lu Min, Lu Qing-Shan, Huang Guo-Dong, Li Int J Microbiol Research Article Amphipathic α-helical antimicrobial peptides comprise a class of broad-spectrum agents that are used against pathogens. We designed a series of antimicrobial peptides, CP-P (KWKSFIKKLTSKFLHLAKKF) and its derivatives, and determined their minimum inhibitory concentrations (MICs) against Pseudomonas aeruginosa, their minimum hemolytic concentrations (MHCs) for human erythrocytes, and the Therapeutic Index (MHC/MIC ratio). We selected the derivative peptide K11, which had the highest therapeutic index (320) among the tested peptides, to determine the MICs against Gram-positive and Gram-negative bacteria and 22 clinical isolates including Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, Pseudomonas aeruginosa, Staphylococcus epidermidis, and Klebsiella pneumonia. K11 exhibited low MICs (less than 10 μg/mL) and broad-spectrum antimicrobial activity, especially against clinically isolated drug-resistant pathogens. Therefore, these results indicate that K11 is a promising candidate antimicrobial peptide for further studies. Hindawi Publishing Corporation 2012 2012-02-16 /pmc/articles/PMC3299254/ /pubmed/22518150 http://dx.doi.org/10.1155/2012/764834 Text en Copyright © 2012 Huang Jin-Jiang et al. https://creativecommons.org/licenses/by/3.0/ 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. |
spellingShingle | Research Article Jin-Jiang, Huang Jin-Chun, Lu Min, Lu Qing-Shan, Huang Guo-Dong, Li The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title | The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title_full | The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title_fullStr | The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title_full_unstemmed | The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title_short | The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide |
title_sort | design and construction of k11: a novel α-helical antimicrobial peptide |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299254/ https://www.ncbi.nlm.nih.gov/pubmed/22518150 http://dx.doi.org/10.1155/2012/764834 |
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