ArticleMolecular pharmaceutics2025
Impact of Lipid Bilayer Composition and Physicochemical Properties on Constitution of a Transmembrane Helical Peptide into Exosome-Mimetic Vesicles.
Article in Molecular pharmaceutics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exosomes are expected to efficiently deliver drugs, such as microRNAs and proteins, to targeted organs. However, using natural exosomes presents many difficulties in terms of safety, quality control, and manufacturing; therefore, developing exosome-mimetic artificial materials is desirable. In this study, we elucidated how sphingomyelin (SM) and cholesterol (CH), the main constituents of the exosome membrane, in addition to phosphatidylcholine (PC), influence the physicochemical properties of PC vesicles. Then, the relevance of these properties to the secondary structure and insertion efficiency of a helical peptide, the transmembrane domain of integrin α, was investigated. The constitution of this peptide was most successful with exosome-mimetic vesicles (EMV) bearing 15 mol % SM and 40 mol % CH, and the exclusion of SM or CH resulted in low dispersion stability or unsuccessful peptide constitution. Physicochemical analysis of the membrane properties revealed that successful peptide incorporation into the lipid membrane relied on the membrane softness induced by CH and the appearance of a highly mobile boundary phase induced by SM, which together created a favorable environment for the peptide. These results provide important insights that serve as a foundation for developing EMV as drug carriers.
Indexed as
Identifiers
What OpenQuestion holds
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.