ArticleJournal of peptide science : an official publication of the European Peptide Society2025
Interactions of Peptide Amphiphiles With Viruses and Cells Are Enabled by Amorphous Nanostructures.
Article in Journal of peptide science : an official publication of the European Peptide Society, 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.
- Interactions of Peptide Amphiphiles With Viruses and Cells Are Enabled by Amorphous Nanostructures.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Peptide amphiphiles can form fibrillar and amorphous structures. While fibrillar assemblies have previously been shown to enhance viral infectivity or retroviral transduction for gene delivery, we now elucidate the mechanism behind amorphous peptide amphiphiles that promote virus-cell interactions. Using electron microscopy, we reveal that amorphous fragments of polyunsaturated peptide amphiphiles allow for more VLPs to bind directly to the plasma membrane, explaining previously observed efficient viral entry and superior biodegradation compared to state-of-the-art adjuvants. We believe our work highlights the potential of unsaturated fatty acid peptide hybrid materials for clinical applications.
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.