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Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs

Antimicrobial peptides (AMPs) are components in the innate immune system of various organisms, and many AMPs can be found in poisons from animals such as spiders, scorpions, and snakes. The peptide Cupiennin-1a is present in the venom of the spider Cupiennius salei and belongs to a group of peptides...

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Autores principales: Araújo, Rayssa Oliveira, Leite, Michel Lopes, Dutra, Thais Tavares Baraviera, Brito da Cunha, Nicolau, Rezende, Taia Maria Berto, Ramada, Marcelo Henrique Soller, Dias, Simoni Campos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9433906/
https://www.ncbi.nlm.nih.gov/pubmed/36060778
http://dx.doi.org/10.3389/fmicb.2022.850007
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author Araújo, Rayssa Oliveira
Leite, Michel Lopes
Dutra, Thais Tavares Baraviera
Brito da Cunha, Nicolau
Rezende, Taia Maria Berto
Ramada, Marcelo Henrique Soller
Dias, Simoni Campos
author_facet Araújo, Rayssa Oliveira
Leite, Michel Lopes
Dutra, Thais Tavares Baraviera
Brito da Cunha, Nicolau
Rezende, Taia Maria Berto
Ramada, Marcelo Henrique Soller
Dias, Simoni Campos
author_sort Araújo, Rayssa Oliveira
collection PubMed
description Antimicrobial peptides (AMPs) are components in the innate immune system of various organisms, and many AMPs can be found in poisons from animals such as spiders, scorpions, and snakes. The peptide Cupiennin-1a is present in the venom of the spider Cupiennius salei and belongs to a group of peptides called cupiennins. The peptide demonstrated high cytotoxic activity against mammalian cells; thus, aiming to solve this problem, seven analogs were designed (R1a, R1b, R2b, R3b, R6b, R8b, and R10b) based on the primary structure of the peptide Cupiennin 1a, reducing its size and substituting some amino acid residues. The antimicrobial results showed that all Cupiennin 1a analogs displayed antimicrobial activity against the tested bacterial and fungal strains. Cytotoxicity tests demonstrated a decrease in the cytotoxic effect of the analogs when compared to the peptide Cupiennin-1a. The antitumor activity against breast adenocarcinoma lines was observed for all the peptides, displaying a better effect against the MCF-7 and MDAMB-231 cell lines. The eight peptides have insecticidal potential, and the original peptide and analogs R6b, R8b, and R10b showed better efficiency even at low concentrations. The rational design of the analogs led to new molecules displaying activities against different cell types and reduced cytotoxicity toward healthy mammalian cells when compared to the original peptide, demonstrating that this was an interesting approach for the development of molecules with biotechnological potential.
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spelling pubmed-94339062022-09-02 Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs Araújo, Rayssa Oliveira Leite, Michel Lopes Dutra, Thais Tavares Baraviera Brito da Cunha, Nicolau Rezende, Taia Maria Berto Ramada, Marcelo Henrique Soller Dias, Simoni Campos Front Microbiol Microbiology Antimicrobial peptides (AMPs) are components in the innate immune system of various organisms, and many AMPs can be found in poisons from animals such as spiders, scorpions, and snakes. The peptide Cupiennin-1a is present in the venom of the spider Cupiennius salei and belongs to a group of peptides called cupiennins. The peptide demonstrated high cytotoxic activity against mammalian cells; thus, aiming to solve this problem, seven analogs were designed (R1a, R1b, R2b, R3b, R6b, R8b, and R10b) based on the primary structure of the peptide Cupiennin 1a, reducing its size and substituting some amino acid residues. The antimicrobial results showed that all Cupiennin 1a analogs displayed antimicrobial activity against the tested bacterial and fungal strains. Cytotoxicity tests demonstrated a decrease in the cytotoxic effect of the analogs when compared to the peptide Cupiennin-1a. The antitumor activity against breast adenocarcinoma lines was observed for all the peptides, displaying a better effect against the MCF-7 and MDAMB-231 cell lines. The eight peptides have insecticidal potential, and the original peptide and analogs R6b, R8b, and R10b showed better efficiency even at low concentrations. The rational design of the analogs led to new molecules displaying activities against different cell types and reduced cytotoxicity toward healthy mammalian cells when compared to the original peptide, demonstrating that this was an interesting approach for the development of molecules with biotechnological potential. Frontiers Media S.A. 2022-08-18 /pmc/articles/PMC9433906/ /pubmed/36060778 http://dx.doi.org/10.3389/fmicb.2022.850007 Text en Copyright © 2022 Araújo, Leite, Dutra, Brito da Cunha, Rezende, Ramada and Dias. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Araújo, Rayssa Oliveira
Leite, Michel Lopes
Dutra, Thais Tavares Baraviera
Brito da Cunha, Nicolau
Rezende, Taia Maria Berto
Ramada, Marcelo Henrique Soller
Dias, Simoni Campos
Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title_full Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title_fullStr Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title_full_unstemmed Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title_short Evaluation of the biotechnological potential of peptide Cupiennin 1a and analogs
title_sort evaluation of the biotechnological potential of peptide cupiennin 1a and analogs
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9433906/
https://www.ncbi.nlm.nih.gov/pubmed/36060778
http://dx.doi.org/10.3389/fmicb.2022.850007
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