Design of Natterins-based peptides improves antimicrobial and antiviral activities
The 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 antimicro...
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| Language: | English |
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Elsevier
2025-03-01
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| Series: | Biotechnology Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2215017X24000407 |
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| author | Gabrielle L. de Cena Dayane B. Tada Danilo B.M. Lucchi Tiago A.A. Santos Montserrat Heras Maria Juliano Carla Torres Braconi Miguel A.R.B. Castanho Mônica Lopes-Ferreira Katia Conceição |
| author_facet | Gabrielle L. de Cena Dayane B. Tada Danilo B.M. Lucchi Tiago A.A. Santos Montserrat Heras Maria Juliano Carla Torres Braconi Miguel A.R.B. Castanho Mônica Lopes-Ferreira Katia Conceição |
| author_sort | Gabrielle L. de Cena |
| collection | DOAJ |
| description | The 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. |
| format | Article |
| id | doaj-art-db6ce18780fb4344aeb267c8e20a7c95 |
| institution | OA Journals |
| issn | 2215-017X |
| language | English |
| publishDate | 2025-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biotechnology Reports |
| spelling | doaj-art-db6ce18780fb4344aeb267c8e20a7c952025-08-20T02:11:01ZengElsevierBiotechnology Reports2215-017X2025-03-0145e0086710.1016/j.btre.2024.e00867Design of Natterins-based peptides improves antimicrobial and antiviral activitiesGabrielle L. de Cena0Dayane B. Tada1Danilo B.M. Lucchi2Tiago A.A. Santos3Montserrat Heras4Maria Juliano5Carla Torres Braconi6Miguel A.R.B. Castanho7Mônica Lopes-Ferreira8Katia Conceição9Laboratory of Peptide Biochemistry, Universidade Federal de São Paulo (UNIFESP), São José dos Campos, BrazilLaboratory of Nanomaterials and Nanotoxicology, Universidade Federal de São Paulo (UNIFESP), São José dos Campos, BrazilDepartment of Microbiology, Immunology and Parasitology, Escola Paulista de Medicina (UNIFESP), São Paulo, BrazilInstituto de Medicina Molecular, Faculdade de Medicina da Universidade de Lisboa, Av. Professor Egas Moniz, 1649-028 Lisboa, PortugalDepartament de Química, Universitat de Girona, Campus Montilivi, 17071 Girona, SpainDepartment of Biophysics, Escola Paulista de Medicina (UNIFESP), São Paulo, BrazilDepartment of Microbiology, Immunology and Parasitology, Escola Paulista de Medicina (UNIFESP), São Paulo, BrazilInstituto de Medicina Molecular, Faculdade de Medicina da Universidade de Lisboa, Av. Professor Egas Moniz, 1649-028 Lisboa, PortugalImmunoregulation Unit, Laboratory of Applied Toxinology (CeTICs/FAPESP), Butantan Institute, São Paulo 05503900, BrazilLaboratory of Peptide Biochemistry, Universidade Federal de São Paulo (UNIFESP), São José dos Campos, Brazil; Corresponding author at: Universidade Federal de São Paulo – UNIFESP, Rua Talim, 330, 12231-280. São José dos Campos, Brazil.The 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.http://www.sciencedirect.com/science/article/pii/S2215017X24000407Bioactive peptidesAntimicrobial peptidesCell penetrating peptidesIn silico predictionADMET |
| spellingShingle | Gabrielle L. de Cena Dayane B. Tada Danilo B.M. Lucchi Tiago A.A. Santos Montserrat Heras Maria Juliano Carla Torres Braconi Miguel A.R.B. Castanho Mônica Lopes-Ferreira Katia Conceição Design of Natterins-based peptides improves antimicrobial and antiviral activities Biotechnology Reports Bioactive peptides Antimicrobial peptides Cell penetrating peptides In silico prediction ADMET |
| title | Design of Natterins-based peptides improves antimicrobial and antiviral activities |
| title_full | Design of Natterins-based peptides improves antimicrobial and antiviral activities |
| title_fullStr | Design of Natterins-based peptides improves antimicrobial and antiviral activities |
| title_full_unstemmed | Design of Natterins-based peptides improves antimicrobial and antiviral activities |
| title_short | Design of Natterins-based peptides improves antimicrobial and antiviral activities |
| title_sort | design of natterins based peptides improves antimicrobial and antiviral activities |
| topic | Bioactive peptides Antimicrobial peptides Cell penetrating peptides In silico prediction ADMET |
| url | http://www.sciencedirect.com/science/article/pii/S2215017X24000407 |
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