ArticleBiochemistry2026
Comparison of Pleated and Rippled β-Sheet Assembly of Sequence Isomers of an Amphipathic Self-Assembling Peptide.
Article in Biochemistry, 2026. 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
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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.
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.
- Aggregation of Amyloid-like Peptides in Different Solvents.Journal of molecular liquids · 2026Article
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Authors and funding
9 authors.
Funding
Abstract
Supramolecular β-sheet peptide nanomaterials are of critical interest due to their relevance in amyloid disorders and are increasingly valued for applications in regenerative medicine, tissue engineering, and antimicrobial design. Amphipathic peptides, particularly those with alternating hydrophobic and hydrophilic residues, readily form amyloid-like pleated β-sheet fibrils. It has been demonstrated that the amino acid sequence order of isomeric peptides dramatically influences the self-assembly propensity of the resulting sequences as well as the morphology of the assembled pleated β-sheet nanomaterials. This was substantiated by our previous investigations of the peptides Ac-(FKFE)
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Registered trials
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