ArticleThe journal of physical chemistry. B2005
Interactions of membrane-active peptides with thick, neutral, nonzwitterionic bilayers.
Article in The journal of physical chemistry. B, 2005. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- Possible Role of Bent Structure of Methylated Lithocholic Acid on Artificial and Plasma Membranes.Membranes · 2022Article
- Article
- Simple surface functionalization of polymersomes using non-antibacterial peptide anchors.Journal of nanobiotechnology · 2016Article
- Review
- Combined cancer photothermal-chemotherapy based on doxorubicin/gold nanorod-loaded polymersomes.Theranostics · 2015Article
- Natural channel protein inserts and functions in a completely artificial, solid-supported bilayer membrane.Scientific reports · 2013Article
- Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.Materials science & engineering. R, Reports : a review journal · 2007Article
- Emerging Applications of Polymersomes in Delivery: from Molecular Dynamics to Shrinkage of Tumors.Progress in polymer science · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Alamethicin is a well-studied channel-forming peptide that has a prototypical amphipathic helix structure. It permeabilizes both microbial and mammalian cell membranes, causing loss of membrane polarization and leakage of endogenous contents. Antimicrobial peptide-lipid systems have been studied quite extensively and have led to significant advancements in membrane biophysics. These studies have been performed on lipid bilayers that are generally charged or zwitterionic and restricted to a thickness range of 3-5 nm. Bilayers of amphiphilic diblock copolymers are a relatively new class of membranes that can have significantly different physicochemical properties compared with those of lipid membranes. In particular, they can be made uncharged, nonzwitterionic, and much thicker than their lipid counterparts. In an effort to extend studies of membrane-protein interactions to these synthetic membranes, we have characterized the interactions of alamethicin and several other membrane-active peptides with diblock copolymer bilayers. We find that although alamethicin is too small to span the bilayer, the peptide interacts with, and ruptures, thick polymer membranes.
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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.