ArticleBiochemistry2010
De novo self-assembling collagen heterotrimers using explicit positive and negative design.
Article in Biochemistry, 2010. 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
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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
20 citing papers in PubMed, 40 citations in OpenAlex.
- De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps.Angewandte Chemie (International ed. in English) · 2023Article
- Article
- Predicting the stability of homotrimeric and heterotrimeric collagen helices.Nature chemistry · 2021Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- How electrostatic networks modulate specificity and stability of collagen.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Multicomponent peptide assemblies.Chemical Society reviews · 2018Review
- ISAMBARD: an open-source computational environment for biomolecular analysis, modelling and design.Bioinformatics (Oxford, England) · 2017Article
- Searching for the Pareto frontier in multi-objective protein design.Biophysical reviews · 2017Review
- NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.The Journal of biological chemistry · 2015Article
- Metal Stabilization of Collagen and de Novo Designed Mimetic Peptides.Biochemistry · 2015Article
- Empirical estimation of local dielectric constants: Toward atomistic design of collagen mimetic peptides.Biopolymers · 2015Article
- Design of net-charged abc-type collagen heterotrimers.Journal of structural biology · 2014Article
- Control of Collagen Stability and Heterotrimer Specificity through Repulsive Electrostatic Interactions.Biomolecules · 2013Article
- Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.The Journal of biological chemistry · 2013Article
- Sequence recombination improves target specificity in a redesigned collagen peptide abc-type heterotrimer.Proteins · 2013Article
- Compositional control of higher order assembly using synthetic collagen peptides.Journal of the American Chemical Society · 2012Article
- Computational design of self-assembling register-specific collagen heterotrimers.Nature communications · 2012Article
- Computational design of a collagen A:B:C-type heterotrimer.Journal of the American Chemical Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We sought to computationally design model collagen peptides that specifically associate as heterotrimers. Computational design has been successfully applied to the creation of new protein folds and functions. Despite the high abundance of collagen and its key role in numerous biological processes, fibrous proteins have received little attention as computational design targets. Collagens are composed of three polypeptide chains that wind into triple helices. We developed a discrete computational model to design heterotrimer-forming collagen-like peptides. Stability and specificity of oligomerization were concurrently targeted using a combined positive and negative design approach. The sequences of three 30-residue peptides, A, B, and C, were optimized to favor charge-pair interactions in an ABC heterotrimer, while disfavoring the 26 competing oligomers (i.e., AAA, ABB, BCA). Peptides were synthesized and characterized for thermal stability and triple-helical structure by circular dichroism and NMR. A unique A:B:C-type species was not achieved. Negative design was partially successful, with only A + B and B + C competing mixtures formed. Analysis of computed versus experimental stabilities helps to clarify the role of electrostatics and secondary-structure propensities determining collagen stability and to provide important insight into how subsequent designs can be improved.
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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.