ArticleJournal of the American Chemical Society2026
Programmable Steric Control of Collagen Peptide-to-Fiber Assembly.
Article in Journal of the American Chemical Society, 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.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Peptide-based collagen-mimetic materials have drawn growing interest as fibrillar collagen surrogates due to their accessibility and versatility. However, an efficient strategy for assembling collagen peptides into well-defined collagen filaments remains elusive, owing to the nonspecific intermolecular interactions in collagen triple-helix formation. Here, we develop a new strategy for designing peptides that form triple-helical collagen-mimicking filaments using a single-residue side-chain modification. By organizing the intermolecular steric interactions in a "bump-gap" design, the peptides self-assemble into interlocked, endlessly growing triple-helical filaments with exceptional specificity. The peptide filaments exhibit high aspect ratios with micrometer lengths and are capable of forming networked structures that build hydrogels. These collagen-mimicking hydrogels, triggered by pH-dependent self-assembly, demonstrate superior stiffness over natural collagen with remarkable shear-thinning properties.
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Registered trials
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