ArticleScientific reports2015
Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 65 citations in OpenAlex.
- Nonspecific interactions can lead to liquid-liquid phase separation in coiled-coil proteins models.bioRxiv : the preprint server for biology · 2025Article
- Coiled Coil Peptide Tiles (CCPTs): Expanding the Peptide Building Block Design with Multivalent Peptide Macrocycles.Journal of the American Chemical Society · 2024Article
- Plant-Produced Viral Nanoparticles as a Functionalized Catalytic Support for Metabolic Engineering.Plants (Basel, Switzerland) · 2024Article
- Bind&Bite: covalently stabilized heterodimeric coiled-coil peptides for the site-selective, cysteine-free chemical modification of proteins.RSC chemical biology · 2023Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- Prerequisites for Stabilizing Long-Range Synergistic Interactions amongBiochemistry · 2022Article
- Nanoscale Structures and Materials from the Self-assembly of Polypeptides and DNA.Current topics in medicinal chemistry · 2022Review
- Liposome fusion with orthogonal coiled coil peptides as fusogens: the efficacy of roleplaying peptides.Chemical science · 2021Article
- Repair of Peripheral Nerve Injury Using Hydrogels Based on Self-Assembled Peptides.Gels (Basel, Switzerland) · 2021Review
- Bioinspired Histidine⁻ZnBiomimetics (Basel, Switzerland) · 2019Article
- Self-assembly in elastin-like recombinamers: a mechanism to mimic natural complexity.Materials today. Bio · 2019Review
- Multicomponent peptide assemblies.Chemical Society reviews · 2018Review
- Kinetic studies on strand displacement inChemical science · 2018Article
- Functional Alleles of Chicken BG Genes, Members of the Butyrophilin Gene Family, in Peripheral T Cells.Frontiers in immunology · 2018Article
- α-Helical coiled-coil peptide materials for biomedical applications.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017Review
- Self-assembly of keratin peptides: Its implication on the performance of electrospun PVA nanofibers.Scientific reports · 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
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coiled coils with defined assembly properties and dissociation constants are highly attractive components in synthetic biology and for fabrication of peptide-based hybrid nanomaterials and nanostructures. Complex assemblies based on multiple different peptides typically require orthogonal peptides obtained by negative design. Negative design does not necessarily exclude formation of undesired species and may eventually compromise the stability of the desired coiled coils. This work describe a set of four promiscuous 28-residue de novo designed peptides that heterodimerize and fold into parallel coiled coils. The peptides are non-orthogonal and can form four different heterodimers albeit with large differences in affinities. The peptides display dissociation constants for dimerization spanning from the micromolar to the picomolar range. The significant differences in affinities for dimerization make the peptides prone to thermodynamic social self-sorting as shown by thermal unfolding and fluorescence experiments, and confirmed by simulations. The peptides self-sort with high fidelity to form the two coiled coils with the highest and lowest affinities for heterodimerization. The possibility to exploit self-sorting of mutually complementary peptides could hence be a viable approach to guide the assembly of higher order architectures and a powerful strategy for fabrication of dynamic and tuneable nanostructured materials.
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.