ArticleBiochemistry2011
What determines the activity of antimicrobial and cytolytic peptides in model membranes.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed.
- A unified model of transient poration induced by antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes.Biochimica et biophysica acta. Biomembranes · 2018Article
- Melittin-Induced Permeabilization, Re-sealing, and Re-permeabilization of E. coli Membranes.Biophysical journal · 2018Article
- Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 2016Article
- Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.Biophysical journal · 2016Article
- Peptides with the same composition, hydrophobicity, and hydrophobic moment bind to phospholipid bilayers with different affinities.The journal of physical chemistry. B · 2014Article
- Membrane-active peptides: binding, translocation, and flux in lipid vesicles.Biochimica et biophysica acta · 2014Review
- Implicit membrane treatment of buried charged groups: application to peptide translocation across lipid bilayers.Biochimica et biophysica acta · 2014Article
- Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state.PloS one · 2014Article
- Translocation of cationic amphipathic peptides across the membranes of pure phospholipid giant vesicles.Journal of the American Chemical Society · 2013Article
- Localized permeabilization of E. coli membranes by the antimicrobial peptide Cecropin A.Biochemistry · 2013Article
- Statistical analysis of peptide-induced graded and all-or-none fluxes in giant vesicles.Biophysical journal · 2013Article
- Hemolytic activity of membrane-active peptides correlates with the thermodynamics of binding to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayers.The Journal of membrane biology · 2013Article
- Activity determinants of helical antimicrobial peptides: a large-scale computational study.PloS one · 2013Article
- Unusual titration of the membrane-bound artificial hemagglutinin fusion peptide.European biophysics journal : EBJ · 2012Article
- Interaction of nuclease colicins with membranes: insertion depth correlates with bilayer perturbation.PloS one · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We previously proposed three hypotheses relating the mechanism of antimicrobial and cytolytic peptides in model membranes to the Gibbs free energies of binding and insertion into the membrane [Almeida, P. F., and Pokorny, A. (2009) Biochemistry 48, 8083-8093]. Two sets of peptides were designed to test those hypotheses, by mutating of the sequences of δ-lysin, cecropin A, and magainin 2. Peptide binding and activity were measured on phosphatidylcholine membranes. In the first set, the peptide charge was changed by mutating basic to acidic residues or vice versa, but the amino acid sequence was not altered much otherwise. The type of dye release changed from graded to all-or-none according to prediction. However, location of charged residues in the sequence with the correct spacing to form salt bridges failed to improve binding. In the second set, the charged and other key residues were kept in the same positions, whereas most of the sequence was significantly but conservatively simplified, maintaining the same hydrophobicity and amphipathicity. This set behaved completely different from predicted. The type of release, which was expected to be maintained, changed dramatically from all-or-none to graded in the mutants of cecropin and magainin. Finally, contrary to the hypotheses, the results indicate that the Gibbs energy of binding to the membrane, not the Gibbs energy of insertion, is the primary determinant of peptide activity.
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Registered trials
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