Structure and function of a novel antioxidant peptide from the skin of tropical frogs

Detalhes bibliográficos
Autor(a) principal: Barbosa, Eder Alves
Data de Publicação: 2018
Outros Autores: Oliveira, Ana, Plácido, Alexandra, Socodato, Renato, Portugal, Camila C., Mafud, Ana Carolina, Ombredane, Alicia S., Moreira, Daniel C., Vale, Nuno, Bessa, Lucinda J., Joanitti, Graziella A., Alves, Cláudia, Gomes, Paula, Delerue-Matos, Cristina, Mascarenhas, Yvonne Primerano, Marani, Mariela M., Relvas, João B., Pintado, Manuela, Leite, José Roberto S.A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.22/15356
Resumo: The amphibian skin plays an important role protecting the organism from external harmful factors such as microorganisms or UV radiation. Based on biorational strategies, many studies have investigated the cutaneous secretion of anurans as a source of bioactive molecules. By a peptidomic approach, a novel antioxidant peptide (AOP) with in vitro free radical scavenging ability was isolated from Physalaemus nattereri. The AOP, named antioxidin-I, has a molecular weight [M+H]+ = 1543.69Da and a TWYFITPYIPDK primary amino acid sequence. The gene encoding the antioxidin-I precursor was expressed in the skin tissue of three other Tropical frog species: Phyllomedusa tarsius, P. distincta and Pithecopus rohdei. cDNA sequencing revealed highly homologous regions (signal peptide and acidic region). Mature antioxidin-I has a novel primary sequence with low similarity compared with previously described amphibian's AOPs. Antioxidin-I adopts a random structure even at high concentrations of hydrophobic solvent, it has poor antimicrobial activity and poor performance in free radical scavenging assays in vitro, with the exception of the ORAC assay. However, antioxidin-I presented a low cytotoxicity and suppressed menadione-induced redox imbalance when tested with fibroblast in culture. In addition, it had the capacity to substantially attenuate the hypoxia-induced production of reactive oxygen species when tested in hypoxia exposed living microglial cells, suggesting a potential neuroprotective role for this peptide.
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spelling Structure and function of a novel antioxidant peptide from the skin of tropical frogsAmphibian ProteinsAnimalsAntimicrobial Cationic PeptidesAntioxidantsAnuraBacterial InfectionsCloning, MolecularFibroblastsFree Radical ScavengersMiceMicrogliaMolecular StructureNIH 3T3 CellsNeuroprotectionOxidation-ReductionProtein ConformationReactive Oxygen SpeciesSkinThe amphibian skin plays an important role protecting the organism from external harmful factors such as microorganisms or UV radiation. Based on biorational strategies, many studies have investigated the cutaneous secretion of anurans as a source of bioactive molecules. By a peptidomic approach, a novel antioxidant peptide (AOP) with in vitro free radical scavenging ability was isolated from Physalaemus nattereri. The AOP, named antioxidin-I, has a molecular weight [M+H]+ = 1543.69Da and a TWYFITPYIPDK primary amino acid sequence. The gene encoding the antioxidin-I precursor was expressed in the skin tissue of three other Tropical frog species: Phyllomedusa tarsius, P. distincta and Pithecopus rohdei. cDNA sequencing revealed highly homologous regions (signal peptide and acidic region). Mature antioxidin-I has a novel primary sequence with low similarity compared with previously described amphibian's AOPs. Antioxidin-I adopts a random structure even at high concentrations of hydrophobic solvent, it has poor antimicrobial activity and poor performance in free radical scavenging assays in vitro, with the exception of the ORAC assay. However, antioxidin-I presented a low cytotoxicity and suppressed menadione-induced redox imbalance when tested with fibroblast in culture. In addition, it had the capacity to substantially attenuate the hypoxia-induced production of reactive oxygen species when tested in hypoxia exposed living microglial cells, suggesting a potential neuroprotective role for this peptide.The authors thank of the B2Tech platform facilities (Biochemical And Biophysical Technologies, Instituto de Investigação e Inovação em Saúde (I3S) da Universidade do Porto, Portugal) for the use of circular dichroism (CD). AP is grateful for the Fundação para a Ciência e a Tecnologia (FCT, Portugal) grants (SFRH/BD/97995/2013) financed by POPH-QREN (subsidized by FSE and MCTES). NV thanks FCT and FEDER (European Union) for funding through UID/MULTI/04378/2013, project grant IF/00092/2014 and IF2014 position. NV thanks also Fundação Manuel António da Mota (FMAM, Portugal) by support to Nuno Vale Lab. PG thanks FCT for funding through UID/QUI/50006/2013. RS and CCP, hold postdoctoral fellowships from FCT (Refs: SFRH/BPD/91833/2012 and FRH/BPD/91962/2012, respectively). ACM is grateful to FAPESP (Grants 2014/02282-6 and 2016/18023-5). YPM is grateful to CNPq by the Senior Researcher Grant (PQ-Sr 306036/2016-9). EAB is grateful to PNPD/CAPES (Grant No:1603966) for its postdoctoral fellowship. M. M. Marani is a researcher at CONICET.ElsevierRepositório Científico do Instituto Politécnico do PortoBarbosa, Eder AlvesOliveira, AnaPlácido, AlexandraSocodato, RenatoPortugal, Camila C.Mafud, Ana CarolinaOmbredane, Alicia S.Moreira, Daniel C.Vale, NunoBessa, Lucinda J.Joanitti, Graziella A.Alves, CláudiaGomes, PaulaDelerue-Matos, CristinaMascarenhas, Yvonne PrimeranoMarani, Mariela M.Relvas, João B.Pintado, ManuelaLeite, José Roberto S.A.2020-01-23T15:05:56Z2018-022018-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.22/15356eng0891-584910.1016/j.freeradbiomed.2017.11.001info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-13T12:57:49Zoai:recipp.ipp.pt:10400.22/15356Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T17:34:15.543667Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Structure and function of a novel antioxidant peptide from the skin of tropical frogs
title Structure and function of a novel antioxidant peptide from the skin of tropical frogs
spellingShingle Structure and function of a novel antioxidant peptide from the skin of tropical frogs
Barbosa, Eder Alves
Amphibian Proteins
Animals
Antimicrobial Cationic Peptides
Antioxidants
Anura
Bacterial Infections
Cloning, Molecular
Fibroblasts
Free Radical Scavengers
Mice
Microglia
Molecular Structure
NIH 3T3 Cells
Neuroprotection
Oxidation-Reduction
Protein Conformation
Reactive Oxygen Species
Skin
title_short Structure and function of a novel antioxidant peptide from the skin of tropical frogs
title_full Structure and function of a novel antioxidant peptide from the skin of tropical frogs
title_fullStr Structure and function of a novel antioxidant peptide from the skin of tropical frogs
title_full_unstemmed Structure and function of a novel antioxidant peptide from the skin of tropical frogs
title_sort Structure and function of a novel antioxidant peptide from the skin of tropical frogs
author Barbosa, Eder Alves
author_facet Barbosa, Eder Alves
Oliveira, Ana
Plácido, Alexandra
Socodato, Renato
Portugal, Camila C.
Mafud, Ana Carolina
Ombredane, Alicia S.
Moreira, Daniel C.
Vale, Nuno
Bessa, Lucinda J.
Joanitti, Graziella A.
Alves, Cláudia
Gomes, Paula
Delerue-Matos, Cristina
Mascarenhas, Yvonne Primerano
Marani, Mariela M.
Relvas, João B.
Pintado, Manuela
Leite, José Roberto S.A.
author_role author
author2 Oliveira, Ana
Plácido, Alexandra
Socodato, Renato
Portugal, Camila C.
Mafud, Ana Carolina
Ombredane, Alicia S.
Moreira, Daniel C.
Vale, Nuno
Bessa, Lucinda J.
Joanitti, Graziella A.
Alves, Cláudia
Gomes, Paula
Delerue-Matos, Cristina
Mascarenhas, Yvonne Primerano
Marani, Mariela M.
Relvas, João B.
Pintado, Manuela
Leite, José Roberto S.A.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Científico do Instituto Politécnico do Porto
dc.contributor.author.fl_str_mv Barbosa, Eder Alves
Oliveira, Ana
Plácido, Alexandra
Socodato, Renato
Portugal, Camila C.
Mafud, Ana Carolina
Ombredane, Alicia S.
Moreira, Daniel C.
Vale, Nuno
Bessa, Lucinda J.
Joanitti, Graziella A.
Alves, Cláudia
Gomes, Paula
Delerue-Matos, Cristina
Mascarenhas, Yvonne Primerano
Marani, Mariela M.
Relvas, João B.
Pintado, Manuela
Leite, José Roberto S.A.
dc.subject.por.fl_str_mv Amphibian Proteins
Animals
Antimicrobial Cationic Peptides
Antioxidants
Anura
Bacterial Infections
Cloning, Molecular
Fibroblasts
Free Radical Scavengers
Mice
Microglia
Molecular Structure
NIH 3T3 Cells
Neuroprotection
Oxidation-Reduction
Protein Conformation
Reactive Oxygen Species
Skin
topic Amphibian Proteins
Animals
Antimicrobial Cationic Peptides
Antioxidants
Anura
Bacterial Infections
Cloning, Molecular
Fibroblasts
Free Radical Scavengers
Mice
Microglia
Molecular Structure
NIH 3T3 Cells
Neuroprotection
Oxidation-Reduction
Protein Conformation
Reactive Oxygen Species
Skin
description The amphibian skin plays an important role protecting the organism from external harmful factors such as microorganisms or UV radiation. Based on biorational strategies, many studies have investigated the cutaneous secretion of anurans as a source of bioactive molecules. By a peptidomic approach, a novel antioxidant peptide (AOP) with in vitro free radical scavenging ability was isolated from Physalaemus nattereri. The AOP, named antioxidin-I, has a molecular weight [M+H]+ = 1543.69Da and a TWYFITPYIPDK primary amino acid sequence. The gene encoding the antioxidin-I precursor was expressed in the skin tissue of three other Tropical frog species: Phyllomedusa tarsius, P. distincta and Pithecopus rohdei. cDNA sequencing revealed highly homologous regions (signal peptide and acidic region). Mature antioxidin-I has a novel primary sequence with low similarity compared with previously described amphibian's AOPs. Antioxidin-I adopts a random structure even at high concentrations of hydrophobic solvent, it has poor antimicrobial activity and poor performance in free radical scavenging assays in vitro, with the exception of the ORAC assay. However, antioxidin-I presented a low cytotoxicity and suppressed menadione-induced redox imbalance when tested with fibroblast in culture. In addition, it had the capacity to substantially attenuate the hypoxia-induced production of reactive oxygen species when tested in hypoxia exposed living microglial cells, suggesting a potential neuroprotective role for this peptide.
publishDate 2018
dc.date.none.fl_str_mv 2018-02
2018-02-01T00:00:00Z
2020-01-23T15:05:56Z
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://hdl.handle.net/10400.22/15356
url http://hdl.handle.net/10400.22/15356
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0891-5849
10.1016/j.freeradbiomed.2017.11.001
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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