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Encrypted Antimicrobial Peptides from Plant Proteins
Examples of bioactive peptides derived from internal sequences of proteins are known for decades. The great majority of these findings appear to be fortuitous rather than the result of a deliberate and methodological-based enterprise. In the present work, we describe the identification and the biolo...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5643462/ https://www.ncbi.nlm.nih.gov/pubmed/29038449 http://dx.doi.org/10.1038/s41598-017-13685-6 |
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author | Ramada, M. H. S. Brand, G. D. Abrão, F. Y. Oliveira, M. Filho, J. L. Cardozo Galbieri, R. Gramacho, K. P. Prates, M. V. Bloch, C. |
author_facet | Ramada, M. H. S. Brand, G. D. Abrão, F. Y. Oliveira, M. Filho, J. L. Cardozo Galbieri, R. Gramacho, K. P. Prates, M. V. Bloch, C. |
author_sort | Ramada, M. H. S. |
collection | PubMed |
description | Examples of bioactive peptides derived from internal sequences of proteins are known for decades. The great majority of these findings appear to be fortuitous rather than the result of a deliberate and methodological-based enterprise. In the present work, we describe the identification and the biological activities of novel antimicrobial peptides unveiled as internal fragments of various plant proteins founded on our hypothesis-driven search strategy. All putative encrypted antimicrobial peptides were selected based upon their physicochemical properties that were iteratively selected by an in-house computer program named Kamal. The selected peptides were chemically synthesized and evaluated for their interaction with model membranes. Sixteen of these peptides showed antimicrobial activity against human and/or plant pathogens, some with a wide spectrum of activity presenting similar or superior inhibition efficacy when compared to classical antimicrobial peptides (AMPs). These original and previously unforeseen molecules constitute a broader and undisputable set of evidences produced by our group that illustrate how the intragenic concept is a workable reality and should be carefully explored not only for microbicidal agents but also for many other biological functions. |
format | Online Article Text |
id | pubmed-5643462 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56434622017-10-19 Encrypted Antimicrobial Peptides from Plant Proteins Ramada, M. H. S. Brand, G. D. Abrão, F. Y. Oliveira, M. Filho, J. L. Cardozo Galbieri, R. Gramacho, K. P. Prates, M. V. Bloch, C. Sci Rep Article Examples of bioactive peptides derived from internal sequences of proteins are known for decades. The great majority of these findings appear to be fortuitous rather than the result of a deliberate and methodological-based enterprise. In the present work, we describe the identification and the biological activities of novel antimicrobial peptides unveiled as internal fragments of various plant proteins founded on our hypothesis-driven search strategy. All putative encrypted antimicrobial peptides were selected based upon their physicochemical properties that were iteratively selected by an in-house computer program named Kamal. The selected peptides were chemically synthesized and evaluated for their interaction with model membranes. Sixteen of these peptides showed antimicrobial activity against human and/or plant pathogens, some with a wide spectrum of activity presenting similar or superior inhibition efficacy when compared to classical antimicrobial peptides (AMPs). These original and previously unforeseen molecules constitute a broader and undisputable set of evidences produced by our group that illustrate how the intragenic concept is a workable reality and should be carefully explored not only for microbicidal agents but also for many other biological functions. Nature Publishing Group UK 2017-10-16 /pmc/articles/PMC5643462/ /pubmed/29038449 http://dx.doi.org/10.1038/s41598-017-13685-6 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Ramada, M. H. S. Brand, G. D. Abrão, F. Y. Oliveira, M. Filho, J. L. Cardozo Galbieri, R. Gramacho, K. P. Prates, M. V. Bloch, C. Encrypted Antimicrobial Peptides from Plant Proteins |
title | Encrypted Antimicrobial Peptides from Plant Proteins |
title_full | Encrypted Antimicrobial Peptides from Plant Proteins |
title_fullStr | Encrypted Antimicrobial Peptides from Plant Proteins |
title_full_unstemmed | Encrypted Antimicrobial Peptides from Plant Proteins |
title_short | Encrypted Antimicrobial Peptides from Plant Proteins |
title_sort | encrypted antimicrobial peptides from plant proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5643462/ https://www.ncbi.nlm.nih.gov/pubmed/29038449 http://dx.doi.org/10.1038/s41598-017-13685-6 |
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