ArticleACS nano2014
Morphological diversity and polymorphism of self-assembling collagen peptides controlled by length of hydrophobic domains.
Article in ACS nano, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.The Journal of biological chemistry · 2026Article
- Article
- De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Recent advances in extracellular matrix-inspired nanocarriers.Expert opinion on drug delivery · 2025Review
- Collagen Hybridizing Peptides Promote Collagen Fibril GrowthACS applied bio materials · 2025Article
- Self-Assembly Behavior of Collagen and Its Composite Materials: Preparation, Characterizations, and Biomedical Engineering and Allied Applications.Gels (Basel, Switzerland) · 2024Review
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Controllable self-assembly of tyrosine-rich triblock peptides into robust collagen mimetic bioscaffolds for aging skin rejuvenation.Regenerative biomaterials · 2024Article
- Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps.Angewandte Chemie (International ed. in English) · 2023Article
- Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed.Nature communications · 2022Article
- Formation of Microcages from a Collagen Mimetic Peptide via Metal-Ligand Interactions.Molecules (Basel, Switzerland) · 2021Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- Designing a bioactive scaffold from coassembled collagen-laminin short peptide hydrogels for controlling cell behaviour.RSC advances · 2019Article
- Article
- Multicomponent peptide assemblies.Chemical Society reviews · 2018Review
- Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.RSC advances · 2018Article
- Crafting of functional biomaterials by directed molecular self-assembly of triple helical peptide building blocks.Interface focus · 2017Review
- Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions.Organic & biomolecular chemistry · 2017Article
- Peptide tessellation yields micrometre-scale collagen triple helices.Nature chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Synthetic collagen mimetic peptides are used to probe the role of hydrophobic forces in mediating protein self-assembly. Higher order association is an integral property of natural collagens, which assemble into fibers and meshes that comprise the extracellular matrix of connective tissues. The unique triple-helix fold fully exposes two-thirds of positions in the protein to solvent, providing ample opportunities for engineering interaction sites. Inclusion of just a few hydrophobic groups in a minimal peptide promotes a rich variety of self-assembly behaviors, resulting in hundred-nanometer to micron size nanodiscs and nanofibers. Morphology depends primarily on the length of hydrophobic domains. Peptide discs contain lipophilic domains capable of sequestering small hydrophobic dyes. Combining multiple peptide types result in composite structures of discs and fibers ranging from stars to plates-on-a-string. These systems provide valuable tools to shed insight into the fundamental principles underlying hydrophobicity-driven higher order protein association that will facilitate the design of self-assembling systems in biomaterials and nanomedical 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.