Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities

Detalhes bibliográficos
Autor(a) principal: Santos, Melina Cardoso dos [UNESP]
Data de Publicação: 2022
Outros Autores: Tairum, Carlos Abrunhosa, Cabrera, Vitoria Isabela Montanhero [UNESP], Cauz, Ana Carolina Guimarães, Ribeiro, Luiz Fernando [UNESP], Toledo Junior, José Carlos, Toyama, Marcos Hikari [UNESP], Lago, João Henrique Ghilardi, Brocchi, Marcelo, Netto, Luis Eduardo Soares, Oliveira, Marcos Antonio de [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1021/acs.chemrestox.2c00049
http://hdl.handle.net/11449/241042
Resumo: The emergence and re-emergence of bacterial strains resistant to multiple drugs represent a global health threat, and the search for novel biological targets is a worldwide concern. AhpC are enzymes involved in bacterial redox homeostasis by metabolizing diverse kinds of hydroperoxides. In pathogenic bacteria, AhpC are related to several functions, as some isoforms are characterized as virulence factors. However, no inhibitor has been systematically evaluated to date. Here we show that the natural ent-kaurane Adenanthin (Adn) efficiently inhibits AhpC and molecular interactions were explored by computer assisted simulations. Additionally, Adn interferes with growth and potentializes the effect of antibiotics (kanamycin and PMBN), positioning Adn as a promising compound to treat infections caused by multiresistant bacterial strains.
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spelling Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic ActivitiesThe emergence and re-emergence of bacterial strains resistant to multiple drugs represent a global health threat, and the search for novel biological targets is a worldwide concern. AhpC are enzymes involved in bacterial redox homeostasis by metabolizing diverse kinds of hydroperoxides. In pathogenic bacteria, AhpC are related to several functions, as some isoforms are characterized as virulence factors. However, no inhibitor has been systematically evaluated to date. Here we show that the natural ent-kaurane Adenanthin (Adn) efficiently inhibits AhpC and molecular interactions were explored by computer assisted simulations. Additionally, Adn interferes with growth and potentializes the effect of antibiotics (kanamycin and PMBN), positioning Adn as a promising compound to treat infections caused by multiresistant bacterial strains.Instituto de Biociências Universidade Estadual Paulista UNESP, São VicenteDepartamento de Genética e Biologia Evolutiva Instituto de Biociências Universidade de São Paulo São PauloDepartamento de Genética Evolução Microbiologia e Imunologia Instituto de Biologia Universidade Estadual de Campinas UNICAMP, CampinasDepartamento de Química Faculdade de Filosofia Ciências e Letras de Ribeirão Preto Universidade de São Paulo, Ribeirão PretoCentro de Ciências Naturais e Humanas Universidade Federal do ABC, Santo AndréInstituto de Biociências Universidade Estadual Paulista UNESP, São VicenteUniversidade Estadual Paulista (UNESP)Universidade de São Paulo (USP)Universidade Estadual de Campinas (UNICAMP)Universidade Federal do ABC (UFABC)Santos, Melina Cardoso dos [UNESP]Tairum, Carlos AbrunhosaCabrera, Vitoria Isabela Montanhero [UNESP]Cauz, Ana Carolina GuimarãesRibeiro, Luiz Fernando [UNESP]Toledo Junior, José CarlosToyama, Marcos Hikari [UNESP]Lago, João Henrique GhilardiBrocchi, MarceloNetto, Luis Eduardo SoaresOliveira, Marcos Antonio de [UNESP]2023-03-01T20:44:24Z2023-03-01T20:44:24Z2022-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1021/acs.chemrestox.2c00049Chemical Research in Toxicology.1520-50100893-228Xhttp://hdl.handle.net/11449/24104210.1021/acs.chemrestox.2c000492-s2.0-85130731565Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChemical Research in Toxicologyinfo:eu-repo/semantics/openAccess2023-03-01T20:44:25Zoai:repositorio.unesp.br:11449/241042Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-03-01T20:44:25Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
title Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
spellingShingle Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
Santos, Melina Cardoso dos [UNESP]
title_short Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
title_full Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
title_fullStr Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
title_full_unstemmed Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
title_sort Adenanthin Is an Efficient Inhibitor of Peroxiredoxins from Pathogens, Inhibits Bacterial Growth, and Potentiates Antibiotic Activities
author Santos, Melina Cardoso dos [UNESP]
author_facet Santos, Melina Cardoso dos [UNESP]
Tairum, Carlos Abrunhosa
Cabrera, Vitoria Isabela Montanhero [UNESP]
Cauz, Ana Carolina Guimarães
Ribeiro, Luiz Fernando [UNESP]
Toledo Junior, José Carlos
Toyama, Marcos Hikari [UNESP]
Lago, João Henrique Ghilardi
Brocchi, Marcelo
Netto, Luis Eduardo Soares
Oliveira, Marcos Antonio de [UNESP]
author_role author
author2 Tairum, Carlos Abrunhosa
Cabrera, Vitoria Isabela Montanhero [UNESP]
Cauz, Ana Carolina Guimarães
Ribeiro, Luiz Fernando [UNESP]
Toledo Junior, José Carlos
Toyama, Marcos Hikari [UNESP]
Lago, João Henrique Ghilardi
Brocchi, Marcelo
Netto, Luis Eduardo Soares
Oliveira, Marcos Antonio de [UNESP]
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
Universidade de São Paulo (USP)
Universidade Estadual de Campinas (UNICAMP)
Universidade Federal do ABC (UFABC)
dc.contributor.author.fl_str_mv Santos, Melina Cardoso dos [UNESP]
Tairum, Carlos Abrunhosa
Cabrera, Vitoria Isabela Montanhero [UNESP]
Cauz, Ana Carolina Guimarães
Ribeiro, Luiz Fernando [UNESP]
Toledo Junior, José Carlos
Toyama, Marcos Hikari [UNESP]
Lago, João Henrique Ghilardi
Brocchi, Marcelo
Netto, Luis Eduardo Soares
Oliveira, Marcos Antonio de [UNESP]
description The emergence and re-emergence of bacterial strains resistant to multiple drugs represent a global health threat, and the search for novel biological targets is a worldwide concern. AhpC are enzymes involved in bacterial redox homeostasis by metabolizing diverse kinds of hydroperoxides. In pathogenic bacteria, AhpC are related to several functions, as some isoforms are characterized as virulence factors. However, no inhibitor has been systematically evaluated to date. Here we show that the natural ent-kaurane Adenanthin (Adn) efficiently inhibits AhpC and molecular interactions were explored by computer assisted simulations. Additionally, Adn interferes with growth and potentializes the effect of antibiotics (kanamycin and PMBN), positioning Adn as a promising compound to treat infections caused by multiresistant bacterial strains.
publishDate 2022
dc.date.none.fl_str_mv 2022-01-01
2023-03-01T20:44:24Z
2023-03-01T20:44:24Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1021/acs.chemrestox.2c00049
Chemical Research in Toxicology.
1520-5010
0893-228X
http://hdl.handle.net/11449/241042
10.1021/acs.chemrestox.2c00049
2-s2.0-85130731565
url http://dx.doi.org/10.1021/acs.chemrestox.2c00049
http://hdl.handle.net/11449/241042
identifier_str_mv Chemical Research in Toxicology.
1520-5010
0893-228X
10.1021/acs.chemrestox.2c00049
2-s2.0-85130731565
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Chemical Research in Toxicology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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