Membrane interactions of the anuran antimicrobial peptide HSP1-NH2: different aspects of the association to anionic and zwitterionic biomimetic systems

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dc.creatorGomes, Isabela Pereira
dc.creatorSantos, Talita Lopes dos
dc.creatorSouza, Amanda Neves de
dc.creatorNunes, Lúcio Otávio
dc.creatorCardoso, Gabriele de Azevedo
dc.creatorMatos, Carolina Oliveira
dc.creatorTorres, Lívia Mara Fontes Costa
dc.creatorLiao, Luciano Morais
dc.creatorResende, Jarbas Magalhães
dc.creatorVerly, Rodrigo Moreira
dc.date.accessioned2024-02-20T15:25:40Z
dc.date.available2024-02-20T15:25:40Z
dc.date.issued2021
dc.description.abstractStudies have suggested that antimicrobial peptides act by different mechanisms, such as micellisation, self-assembly of nanostructures and pore formation on the membrane surface. This work presents an extensive investigation of the membrane interactions of the 14 amino-acid antimicrobial peptide hylaseptin P1-NH2 (HSP1-NH2), derived from the tree-frog Hyla punctata, which has stronger antifungal than antibacterial potential. Biophysical and structural analyses were performed and the correlated results were used to describe in detail the interactions of HSP1-NH2 with zwitterionic and anionic detergent micelles and phospholipid vesicles. HSP1-NH2 presents similar well-defined helical conformations in both zwitterionic and anionic micelles, although NMR spectroscopy revealed important structural differences in the peptide N-terminus. 2H exchange experiments of HSP1-NH2 indicated the insertion of the most N-terminal residues (1–3) in the DPC-d38 micelles. A higher enthalpic contribution was verified for the interaction of the peptide with anionic vesicles in comparison with zwitterionic vesicles. The pore formation ability of HSP1-NH2 (examined by dye release assays) and its effect on the size and surface charge as well as on the lipid acyl chain ordering (evaluated by Fourier-transform infrared spectroscopy) of anionic phospholipid vesicles showed membrane disruption even at low peptide-to-phospholipid ratios, and the effect increases proportionately to the peptide concentration. On the other hand, these biophysical investigations showed that a critical peptide-to-phospholipid ratio around 0.6 is essential for promoting disruption of zwitterionic membranes. In conclusion, this study demonstrates that the binding process of the antimicrobial HSP1-NH2 peptide depends on the membrane composition and peptide concentration.
dc.identifier.citationGOMES, Isabela P. et al. Membrane interactions of the anuran antimicrobial peptide HSP1-NH2: different aspects of the association to anionic and zwitterionic biomimetic systems. BBA: biomembranes, Amsterdam, v. 1863, n. 1, e183449, 2021. DOI: 10.1016/j.bbamem.2020.183449. Disponível em: https://www.sciencedirect.com/science/article/pii/S0005273620302923?via%3Dihub. Acesso em: 16 fev. 2024.
dc.identifier.doi10.1016/j.bbamem.2020.183449
dc.identifier.issn0005-2736
dc.identifier.issne- 1879-2642
dc.identifier.urihttp://repositorio.bc.ufg.br//handle/ri/24395
dc.language.isoeng
dc.publisher.countryHolanda
dc.publisher.departmentInstituto de Química - IQ (RMG)
dc.rightsAcesso Aberto
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectPeptide-membrane interaction
dc.subjectAntimicrobial peptides
dc.subjectAntimicrobial mechanism of action
dc.subjectConformational analysis of peptides
dc.subjectMembrane active peptides
dc.subjectBiophysical prediction of peptide-membrane interactions
dc.subjectMembrane-dependent composition
dc.titleMembrane interactions of the anuran antimicrobial peptide HSP1-NH2: different aspects of the association to anionic and zwitterionic biomimetic systems
dc.typeArtigo

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