Membrane interactions of the anuran antimicrobial peptide HSP1-NH2: different aspects of the association to anionic and zwitterionic biomimetic systems
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2021
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Studies 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.
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Peptide-membrane interaction, Antimicrobial peptides, Antimicrobial mechanism of action, Conformational analysis of peptides, Membrane active peptides, Biophysical prediction of peptide-membrane interactions, Membrane-dependent composition
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GOMES, 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.