ArticleBiophysical journal2023
The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization.Biophysical journal · 2026Article
- Review
- Amniotic membrane, a novel bioscaffold in cardiac diseases: from mechanism to applications.Frontiers in bioengineering and biotechnology · 2024Review
- Membrane-Active Peptides and Their Potential Biomedical Application.Pharmaceutics · 2023Review
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Authors and funding
5 authors.
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Abstract
Antimicrobial peptides are an important class of membrane-active peptides that can provide alternatives or complements to classic antibiotics. Among the many classes of AMPs, the histidine-rich family is of particular interest since they may induce pH-sensitive interactions with cell membranes. The AMP caerin 1.1 (Cae-1), from Australian tree frogs, has three histidine residues, and thus we studied the pH dependence of its interactions with model cell membranes. Using NMR spectroscopy and molecular dynamics simulations, we showed that Cae-1 induced greater perturbation of the lipid dynamics and water penetrations within the membrane interior in an acidic environment compared with physiological conditions. Using
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