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Design of natterins-based peptides improves antimicrobial and antiviral activities

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dc.contributor.authorde Cena, Gabrielle L.
dc.contributor.authorTada, Dayane B.
dc.contributor.authorLucchi, Danilo B. M.
dc.contributor.authorSantos, Tiago
dc.contributor.authorHeras, Montserrat
dc.contributor.authorJuliano, Maria
dc.contributor.authorTorres Braconi, Carla
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorLopes-Ferreira, Mônica
dc.contributor.authorConceição, Katia
dc.date.accessioned2025-02-11T14:45:50Z
dc.date.available2025-02-11T14:45:50Z
dc.date.issued2025
dc.description© 2024 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).pt_PT
dc.description.abstractThe biochemical analysis of animal venoms has been intensifying over the years, enabling the prediction of new molecules derived from toxins, harnessing the therapeutic potential of these molecules. From the venom of the fish Thalassophryne nattereri, using in silico methods for predicting antimicrobial and cell-penetrating peptides, two peptides from Natterins with promising characteristics were synthesized and subjected to in vitro and in vivo analysis. The peptides were subjected to stability tests and antimicrobial assays, cytotoxicity in murine fibroblast cells, antiviral assays against the Chikungunya virus, and the toxicity on G. mellonella was also evaluated. The findings underscore the peptides' robust stability under varying temperatures and pH conditions and resistance to proteolytic degradation. The peptides demonstrated significant antimicrobial efficacy, minimal cytotoxicity, and low hemolytic activity. Although their antiviral efficacy was limited, they showed potential at specific stages of viral replication. The in vivo toxicity tests indicated a favorable safety profile. These findings suggest that this approach can aid in the development of antimicrobial agents, offering a faster and personalized method to combat microbial infections, and represent a promising discovery in venom biotechnology research.pt_PT
dc.description.sponsorshipThis research used facilities of Laborat´orio Multiusu´ario em Biotecnologia (LMBiotec/UNIFESP).Work supported by the European Union’s Horizon 2020 research and innovation programme under grant agreement No 828774.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBiotechnol Rep (Amst). 2024 Nov 28:45:e00867pt_PT
dc.identifier.doi10.1016/j.btre.2024.e00867pt_PT
dc.identifier.eissn2215-017X
dc.identifier.urihttp://hdl.handle.net/10400.5/98328
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation''One size fits all'' unique drug to eradicate multiple viral species simultaneously from the central nervous system of co-infected individuals
dc.relation.publisherversionhttps://www.sciencedirect.com/journal/biotechnology-reportspt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectADMETpt_PT
dc.subjectAntimicrobial peptidespt_PT
dc.subjectBioactive peptidespt_PT
dc.subjectCell penetrating peptidespt_PT
dc.subjectIn silico predictionpt_PT
dc.titleDesign of natterins-based peptides improves antimicrobial and antiviral activitiespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitle''One size fits all'' unique drug to eradicate multiple viral species simultaneously from the central nervous system of co-infected individuals
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/828774/EU
oaire.citation.titleBiotechnology Reportspt_PT
oaire.citation.volume45pt_PT
oaire.fundingStreamH2020
person.familyNameSantos
person.familyNameCastanho
person.givenNameTiago
person.givenNameMiguel
person.identifier1472898
person.identifier.orcid0000-0003-4620-0174
person.identifier.orcid0000-0001-7891-7562
person.identifier.scopus-author-id57146726700
person.identifier.scopus-author-id56605575600
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication487239a7-23d2-4848-96e4-00c91694db8b
relation.isAuthorOfPublicationf5e46f85-fabf-450a-9ee2-1c7b59410892
relation.isAuthorOfPublication.latestForDiscovery487239a7-23d2-4848-96e4-00c91694db8b
relation.isProjectOfPublicationd1bca66a-13d0-41bd-bd70-f6039a1fbb33
relation.isProjectOfPublication.latestForDiscoveryd1bca66a-13d0-41bd-bd70-f6039a1fbb33

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