ArticleInternational journal of molecular sciences2019
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Combating Fuel Biocontamination: Tailored Antimicrobial Peptides and an Innovative Delivery Strategy.ACS applied bio materials · 2025Article
- Study on antimicrobial activity of sturgeon skin mucus polypeptides (Rational Design, Self-Assembly and Application).Food chemistry: X · 2024Article
- NGIWY-Amide: A Bioinspired Ultrashort Self-Assembled Peptide Gelator for Local Drug Delivery Applications.Pharmaceutics · 2022Article
- Polarimetric Measurements of Surface Chirality Based on Linear and Nonlinear Light Scattering.Frontiers in chemistry · 2020Review
- Self-Association of Antimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin.International journal of molecular sciences · 2019Article
- Polymeric Systems as Antimicrobial or Antifouling Agents.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
We have investigated structural changes of peptides related to antimicrobial peptide Halictine-1 (HAL-1) induced by interaction with various membrane-mimicking models with the aim to identify a mechanism of the peptide mode of action and to find a correlation between changes of primary/secondary structure and biological activity. Modifications in the HAL-1 amino acid sequence at particular positions, causing an increase of amphipathicity (Arg/Lys exchange), restricted mobility (insertion of Pro) and consequent changes in antimicrobial and hemolytic activity, led to different behavior towards model membranes. Secondary structure changes induced by peptide-membrane interaction were studied by circular dichroism, infrared spectroscopy, and fluorescence spectroscopy. The experimental results were complemented by molecular dynamics calculations. An α-helical structure has been found to be necessary but not completely sufficient for the HAL-1 peptides antimicrobial action. The role of alternative conformations (such as β-sheet, PPII or 3
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Registered trials
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