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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...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
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.
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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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