Evidence map›Paper›PMID 26216960›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.

Katelyn Nagy-Smith, Eric Moore, Joel Schneider, Robert Tycko

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Induction and Stabilization of Peptide Alpha-Helices on Silica Nanoparticles.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Article
  4. Substituent-Based Modulation of Self-Assembly and Immunogenicity of Amphipathic Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Review
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  14. Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
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  18. EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Katelyn Nagy-SmithChemical Biology Laboratory, Frederick National Laboratory for Cancer Research, National Cancer Institute, Frederick, MD 21702; Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716;
Eric MooreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Joel SchneiderChemical Biology Laboratory, Frederick National Laboratory for Cancer Research, National Cancer Institute, Frederick, MD 21702;
Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 robertty@mail.nih.gov.

Funding

Design and Utility of Novel Protienaceous BiomaterialsZIABC011313 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$19.0M
Development of antibacterial agents and materialsZIABC011314 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$8.9M
Structural Studies of Prion Fibrils and Other Protein FibrilsZIADK075031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$7.3M
Intramural NIH HHS
6 · The paper itself

Abstract

Most, if not all, peptide- and protein-based hydrogels formed by self-assembly can be characterized as kinetically trapped 3D networks of fibrils. The propensity of disease-associated amyloid-forming peptides and proteins to assemble into polymorphic fibrils suggests that cross-β fibrils comprising hydrogels may also be polymorphic. We use solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. We find that MAX1 adopts a β-hairpin conformation and self-assembles with high fidelity into a double-layered cross-β structure. Hairpins assemble with an in-register Syn orientation within each β-sheet layer and with an Anti orientation between layers. Surprisingly, although the MAX1 fibril network is kinetically trapped, solid-state NMR data show that fibrils within this network are monomorphic and most likely represent the thermodynamic ground state. Intermolecular interactions not available in alternative structural arrangements apparently dictate this monomorphic behavior.

Indexed as

Models, MolecularHydrogel, Polyethylene Glycol DimethacrylateIsotope LabelingKineticsMagnetic Resonance SpectroscopyMicroscopy, Electron, TransmissionPeptidesProtein Structure, SecondaryHydrogel, Polyethylene Glycol DimethacrylatePeptidesamyloidcross-β structurepeptide designpolymorphismβ-hairpin

Identifiers

PMID26216960
PMCPMC4538636

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.