Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides

Antimicrobial peptides have been developed based on plant-derived molecular scaffolds for the treatment of infectious diseases. Chenopodin is an abundant seed storage protein in quinoa, an Andean plant with high nutritional and therapeutic properties. Here, we used computer- and physicochemical-base...

Cur síos iomlán

Sábháilte in:
Sonraí bibleagrafaíochta
Príomhchruthaitheoir: Espinosa de los Monteros Silva, Nina (author)
Rannpháirtithe: Proaño Bolaños, Carolina (author), de Almeida, José R. (author), Feijoo-Coronel, Marcia L. (author), Mendes, Bruno (author), Ramírez, David (author), Peña-Varas, Carlos (author), de Oliveira, Leonardo Camilo (author), Fernandes Lívio, Diego (author), da Silva, José Antônio (author), F. da Silva, José Maurício S. (author), G. Pereira, Marília Gabriella A. (author), B. Rodrigues, Marina Q. R. (author), Teixeira, Mauro M. (author), Granjeiro, Paulo Afonso (author), Patel, Ketan (author), Vaiyapuri, Sakthivel (author)
Formáid: article
Foilsithe / Cruthaithe: 2024
Ábhair:
Rochtain ar líne:https://doi.org/10.3390/antibiotics13010078
http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/770
Clibeanna: Cuir clib leis
Níl clibeanna ann, Bí ar an gcéad duine le clib a chur leis an taifead seo!
_version_ 1858435696017014784
author Espinosa de los Monteros Silva, Nina
author2 Proaño Bolaños, Carolina
de Almeida, José R.
Feijoo-Coronel, Marcia L.
Mendes, Bruno
Ramírez, David
Peña-Varas, Carlos
de Oliveira, Leonardo Camilo
Fernandes Lívio, Diego
da Silva, José Antônio
F. da Silva, José Maurício S.
G. Pereira, Marília Gabriella A.
B. Rodrigues, Marina Q. R.
Teixeira, Mauro M.
Granjeiro, Paulo Afonso
Patel, Ketan
Vaiyapuri, Sakthivel
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author_facet Espinosa de los Monteros Silva, Nina
Proaño Bolaños, Carolina
de Almeida, José R.
Feijoo-Coronel, Marcia L.
Mendes, Bruno
Ramírez, David
Peña-Varas, Carlos
de Oliveira, Leonardo Camilo
Fernandes Lívio, Diego
da Silva, José Antônio
F. da Silva, José Maurício S.
G. Pereira, Marília Gabriella A.
B. Rodrigues, Marina Q. R.
Teixeira, Mauro M.
Granjeiro, Paulo Afonso
Patel, Ketan
Vaiyapuri, Sakthivel
author_role author
collection Repositorio Universidad Regional Amazónica
dc.creator.none.fl_str_mv Espinosa de los Monteros Silva, Nina
Proaño Bolaños, Carolina
de Almeida, José R.
Feijoo-Coronel, Marcia L.
Mendes, Bruno
Ramírez, David
Peña-Varas, Carlos
de Oliveira, Leonardo Camilo
Fernandes Lívio, Diego
da Silva, José Antônio
F. da Silva, José Maurício S.
G. Pereira, Marília Gabriella A.
B. Rodrigues, Marina Q. R.
Teixeira, Mauro M.
Granjeiro, Paulo Afonso
Patel, Ketan
Vaiyapuri, Sakthivel
dc.date.none.fl_str_mv 2024-06-11T20:34:09Z
2024-06-11T20:34:09Z
2024
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv 2079-6382
https://doi.org/10.3390/antibiotics13010078
http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/770
dc.language.none.fl_str_mv en
dc.publisher.none.fl_str_mv scopus
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
dc.source.none.fl_str_mv reponame:Repositorio Universidad Regional Amazónica
instname:Universidad Regional Amazónica
instacron:IKIAM
dc.subject.none.fl_str_mv antimicrobial
antiviral
Chenopodin
membranolytic
quinoa
synthetic peptides
dc.title.none.fl_str_mv Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
description Antimicrobial peptides have been developed based on plant-derived molecular scaffolds for the treatment of infectious diseases. Chenopodin is an abundant seed storage protein in quinoa, an Andean plant with high nutritional and therapeutic properties. Here, we used computer- and physicochemical-based strategies and designed four peptides derived from the primary structure of Chenopodin. Two peptides reproduce natural fragments of 14 amino acids from Chenopodin, named Chen1 and Chen2, and two engineered peptides of the same length were designed based on the Chen1 sequence. The two amino acids of Chen1 containing amide side chains were replaced by arginine (ChenR) or tryptophan (ChenW) to generate engineered cationic and hydrophobic peptides. The evaluation of these 14-mer peptides on Staphylococcus aureus and Escherichia coli showed that Chen1 does not have antibacterial activity up to 512 µM against these strains, while other peptides exhibited antibacterial effects at lower concentrations. The chemical substitutions of glutamine and asparagine by amino acids with cationic or aromatic side chains significantly favoured their antibacterial effects. These peptides did not show significant hemolytic activity. The fluorescence microscopy analysis highlighted the membranolytic nature of Chenopodin-derived peptides. Using molecular dynamic simulations, we found that a pore is formed when multiple peptides are assembled in the membrane. Whereas, some of them form secondary structures when interacting with the membrane, allowing water translocations during the simulations. Finally, Chen2 and ChenR significantly reduced SARSCoV-2 infection. These findings demonstrate that Chenopodin is a highly useful template for the design, engineering, and manufacturing of non-toxic, antibacterial, and antiviral peptides.
eu_rights_str_mv openAccess
format article
id IKIAM_d0bfb07aa9bb35bb6677f22f4d26389a
identifier_str_mv 2079-6382
instacron_str IKIAM
institution IKIAM
instname_str Universidad Regional Amazónica
language_invalid_str_mv en
network_acronym_str IKIAM
network_name_str Repositorio Universidad Regional Amazónica
oai_identifier_str oai:repositorio.ikiam.edu.ec:RD_IKIAM/770
publishDate 2024
publisher.none.fl_str_mv scopus
reponame_str Repositorio Universidad Regional Amazónica
repository.mail.fl_str_mv .
repository.name.fl_str_mv Repositorio Universidad Regional Amazónica - Universidad Regional Amazónica
repository_id_str 0
spelling Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic PeptidesEspinosa de los Monteros Silva, NinaProaño Bolaños, Carolinade Almeida, José R.Feijoo-Coronel, Marcia L.Mendes, BrunoRamírez, DavidPeña-Varas, Carlosde Oliveira, Leonardo CamiloFernandes Lívio, Diegoda Silva, José AntônioF. da Silva, José Maurício S.G. Pereira, Marília Gabriella A.B. Rodrigues, Marina Q. R.Teixeira, Mauro M.Granjeiro, Paulo AfonsoPatel, KetanVaiyapuri, SakthivelantimicrobialantiviralChenopodinmembranolyticquinoasynthetic peptidesAntimicrobial peptides have been developed based on plant-derived molecular scaffolds for the treatment of infectious diseases. Chenopodin is an abundant seed storage protein in quinoa, an Andean plant with high nutritional and therapeutic properties. Here, we used computer- and physicochemical-based strategies and designed four peptides derived from the primary structure of Chenopodin. Two peptides reproduce natural fragments of 14 amino acids from Chenopodin, named Chen1 and Chen2, and two engineered peptides of the same length were designed based on the Chen1 sequence. The two amino acids of Chen1 containing amide side chains were replaced by arginine (ChenR) or tryptophan (ChenW) to generate engineered cationic and hydrophobic peptides. The evaluation of these 14-mer peptides on Staphylococcus aureus and Escherichia coli showed that Chen1 does not have antibacterial activity up to 512 µM against these strains, while other peptides exhibited antibacterial effects at lower concentrations. The chemical substitutions of glutamine and asparagine by amino acids with cationic or aromatic side chains significantly favoured their antibacterial effects. These peptides did not show significant hemolytic activity. The fluorescence microscopy analysis highlighted the membranolytic nature of Chenopodin-derived peptides. Using molecular dynamic simulations, we found that a pore is formed when multiple peptides are assembled in the membrane. Whereas, some of them form secondary structures when interacting with the membrane, allowing water translocations during the simulations. Finally, Chen2 and ChenR significantly reduced SARSCoV-2 infection. These findings demonstrate that Chenopodin is a highly useful template for the design, engineering, and manufacturing of non-toxic, antibacterial, and antiviral peptides.scopus2024-06-11T20:34:09Z2024-06-11T20:34:09Z2024info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdf2079-6382https://doi.org/10.3390/antibiotics13010078http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/770eninfo:eu-repo/semantics/openAccessreponame:Repositorio Universidad Regional Amazónicainstname:Universidad Regional Amazónicainstacron:IKIAM2024-06-12T08:00:43Zoai:repositorio.ikiam.edu.ec:RD_IKIAM/770Institucionalhttps://repositorio.ikiam.edu.ec/Universidad públicahttps://www.ikiam.edu.ec/https://repositorio.ikiam.edu.ec/oaiEcuador...opendoar:02024-06-12T08:00:43falseInstitucionalhttps://repositorio.ikiam.edu.ec/Universidad públicahttps://www.ikiam.edu.ec/https://repositorio.ikiam.edu.ec/oai.Ecuador...opendoar:02024-06-12T08:00:43Repositorio Universidad Regional Amazónica - Universidad Regional Amazónicafalse
spellingShingle Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
Espinosa de los Monteros Silva, Nina
antimicrobial
antiviral
Chenopodin
membranolytic
quinoa
synthetic peptides
status_str publishedVersion
title Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
title_full Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
title_fullStr Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
title_full_unstemmed Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
title_short Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
title_sort Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
topic antimicrobial
antiviral
Chenopodin
membranolytic
quinoa
synthetic peptides
url https://doi.org/10.3390/antibiotics13010078
http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/770