ArticleEuropean biophysics journal : EBJ2010
X-ray scattering studies of model lipid membrane interacting with purothionin provide support for a previously proposed mechanism of membrane lysis.
Article in European biophysics journal : EBJ, 2010. 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, 28 citations in OpenAlex.
- Emerging Applications of Plant Antimicrobials in the Food Industry.Current pharmaceutical biotechnology · 2025Review
- X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model.Scientific reports · 2023Article
- Recombinant Fusion Protein Containing Plant Nigellothionin Regulates the Growth of Food-Spoiling Fungus (Foods (Basel, Switzerland) · 2023Article
- Antimicrobial Peptides: Challenging Journey to the Pharmaceutical, Biomedical, and Cosmeceutical Use.International journal of molecular sciences · 2023Review
- The Plant Peptidome: An Expanding Repertoire of Structural Features and Biological Functions.The Plant cell · 2015Review
- Plant antimicrobial peptides.Folia microbiologica · 2014Review
- Properties and mechanisms of action of naturally occurring antifungal peptides.Cellular and molecular life sciences : CMLS · 2013Review
- Amino acid-derived defense metabolites from plants: A potential source to facilitate novel antimicrobial development.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thionins, ubiquitous plant toxins, are believed to act by lysing the membrane of pathogenic organisms. Several competing mechanisms were proposed for the lysis of phospholipid membranes by the toxins. In order to study in more detail the proposed mechanisms and possibly resolve among the competing proposals, the interactions of purothionins with a model lipid membrane in the form of a monolayer were studied. The monolayer formed at the air-water interface was studied by synchrotron X-ray reflectivity and grazing incidents diffraction methods. The model membrane was composed of 90:10 mol% DPPC:DPPS (dipylmitoyl phosphatidylcholine:dipylmitoyl phosphatidylserine). The protein interaction with the monolayer disturbs the in-plane and out-of-plane order of phospholipids, increases the amount of the liquid phase of the monolayer, and increases the average surface area per alkyl chain. The results indicate that the protein is bound only transiently, and after approximately 4 h most of the properties of the monolayer are reminiscent of the pure DPPC monolayer suggesting partial withdrawal of DPPS. Obtained electron density distributions perpendicular to the membrane interface do not show any significant contribution from the adsorbed proteins, further supporting the withdrawal hypothesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.