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Membrane interactions of the anuran antimicrobial peptide HSP1-NH: Different aspects of the association to anionic and zwitterionic biomimetic systems. | LitMetric

AI Article Synopsis

  • Antimicrobial peptides like hylaseptin P1-NH (HSP1-NH) have varying mechanisms for disrupting membranes, and this study focuses on its interactions with zwitterionic and anionic micelles and vesicles.
  • HSP1-NH shows distinct helical structures but reveals structural differences, especially at its N-terminus, when interacting with different membrane types.
  • The peptide disrupts anionic membranes effectively, even at low concentrations, while a specific peptide-to-phospholipid ratio of about 0.6 is necessary for affecting zwitterionic membranes.

Article Abstract

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-NH (HSP1-NH), 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-NH with zwitterionic and anionic detergent micelles and phospholipid vesicles. HSP1-NH presents similar well-defined helical conformations in both zwitterionic and anionic micelles, although NMR spectroscopy revealed important structural differences in the peptide N-terminus. H exchange experiments of HSP1-NH indicated the insertion of the most N-terminal residues (1-3) in the DPC-d 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-NH (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-NH peptide depends on the membrane composition and peptide concentration.

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Source
http://dx.doi.org/10.1016/j.bbamem.2020.183449DOI Listing

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