ArticleThe Journal of antibiotics2018
Effect of antimicrobial peptides from Galleria mellonella on molecular models of Leishmania membrane. Thermotropic and fluorescence anisotropy study.
Article in The Journal of antibiotics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
8 citing papers in PubMed, 16 citations in OpenAlex.
- Peptides as a Therapeutic Alternative Against Leishmaniasis: A Scoping Review.Chemical biology & drug design · 2026Article
- Review
- Evaluation of Beauvericin's activity and mode of action against all life stages ofFrontiers in cellular and infection microbiology · 2025Article
- Review
- Sequential Two-Photon Delayed Fluorescence Anisotropy for Macromolecular Size Determination.The journal of physical chemistry. B · 2023Article
- Bioactive cationic peptides as potential agents for breast cancer treatment.Bioscience reports · 2021Article
- Membrane disruption of Fusarium oxysporum f. sp. niveum induced by myriocin from Bacillus amyloliquefaciens LZN01.Microbial biotechnology · 2021Article
- Trematocine, a Novel Antimicrobial Peptide from the Antarctic FishAntibiotics (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides are molecules of natural origin, produced by organisms such as insects, which have focused attention as potential antiparasitic agents. They can cause the death of parasites such Leishmania by interacting with their membrane. In this study, additional information was obtained on how the anionic peptide 2 and cecropin D-like peptide derived from Galleria mellonella interact with liposomes that mimic the composition of the Leishmania membrane. In order to do this, lipid bilayers consisting of dipalmitoylphosphatidylcholine, dipalmitoylphosphatidylethanolamine, dimyristoylphosphatidylserine, and dimyristoylphosphatidylglycerol were constructed. The effect of the peptides on these membranes was evaluated using calorimetry analysis and fluorescence spectroscopy. The results obtained using differential scanning calorimetry indicated a concentration-dependent effect on membranes composed of phosphatidylserine and phosphatidylglycerol, showing a preference of both peptides for anionic lipids. The binding of the peptides drastically reduced the transition enthalpy in the phosphatidylserine and phosphatidylglycerol liposomes. The results suggest that the mode of action of anionic peptide 2 and cecropin D-like peptide is different, with a higher effect of cecropin D-like on the anionic lipids, which led to changes in the main transition temperature and a complete solubilization of the vesicles. Interactions between peptides and phosphatidylcholine, which is the most abundant lipid on the surface of Leishmania cells, were evaluated using isothermal titration calorimetry and the anisotropy of fluorescence of DPH. The peptides had a slight effect on the gel phase of the phosphatidylcholine, with changes in the anisotropy correlated with that observed by DSC. The results showed a selectivity of these peptides toward some lipids, which will direct the study of the development of new drugs.
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