Evidence map›Paper›PMID 39613762›Full record

ArticleNature communications2024

Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix.

Le Tracy Yu, Mark A B Kreutzberger, Thi H Bui, Maria C Hancu, Adam C Farsheed, Edward H Egelman, Jeffrey D Hartgerink

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. A Collagen Triple Helix without the Super Helical Twist.bioRxiv : the preprint server for biology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Le Tracy YuDepartment of Chemistry, Rice University, Houston, TX, USA.ORCID 0000-0001-9904-6460
Mark A B KreutzbergerDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA, USA.
Thi H BuiDepartment of Chemistry, Rice University, Houston, TX, USA.
Maria C HancuDepartment of Chemistry, Rice University, Houston, TX, USA.
Adam C FarsheedDepartment of Bioengineering, Rice University, Houston, TX, USA.ORCID 0000-0003-0310-2144
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA, USA.ORCID 0000-0003-4844-5212
Jeffrey D HartgerinkDepartment of Chemistry, Rice University, Houston, TX, USA. jdh@rice.edu.ORCID 0000-0002-3186-5395

Funding

Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
NIGMS NIH HHS R35 GM122510Welch Foundation C-2141
6 · The paper itself

Abstract

The de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we focus on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen Surfactant Protein A as a model. By dissecting the sequence derived from Surfactant Protein A and synthesizing short collagen-like peptides, we successfully construct a discrete bundle of hollow triple helices. Amino acid substitution studies pinpoint hydrophobic and charged residues that are critical for oligomer formation. These insights guide the de novo design of collagen-like peptides, resulting in the formation of diverse quaternary structures, including discrete and heterogenous bundled oligomers, two-dimensional nanosheets, and pH-responsive nanoribbons. Our study represents a significant advancement in the understanding and harnessing of collagen higher-order assemblies beyond the triple helix.

Indexed as

CollagenPeptidesAmino Acid SequenceHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsModels, MolecularProtein Conformation, alpha-HelicalProtein Structure, SecondaryCollagenPeptides

Identifiers

PMID39613762
PMCPMC11606958

What OpenQuestion holds

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Registered trials

None linked

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.