Evidence map›Paper›PMID 28691070›Full record

ArticleACS central science2017

Molecular, Local, and Network-Level Basis for the Enhanced Stiffness of Hydrogel Networks Formed from Coassembled Racemic Peptides: Predictions from Pauling and Corey.

Katelyn Nagy-Smith, Peter J Beltramo, Eric Moore, Robert Tycko, Eric M Furst, Joel P Schneider

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.7field-weighted citation impact, top 2% of its field
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

62 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. The Rippled Beta-Sheet: An Old Prediction Inspires a New Field.Chembiochem : a European journal of chemical biology · 2026
    Review
  7. Modulating Peptide Self-Assembly via Triblock Chiral Patterning.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Journal of the American Chemical Society · 2024
    Article
  14. Article
  15. ACS omega · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

2 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

6 authors at 3 institutions in 1 country.

Katelyn Nagy-SmithChemical Biology Laboratory, National Cancer Institute, Frederick, Maryland 21702, United States.
Peter J BeltramoDepartment of Chemistry and Biochemistry and Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware 19716, United States.
Eric MooreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.
Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.
Eric M FurstDepartment of Chemistry and Biochemistry and Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware 19716, United States.
Joel P SchneiderChemical Biology Laboratory, National Cancer Institute, Frederick, Maryland 21702, United States.
Frederick National Laboratory for Cancer Research · USNational Institutes of Health · USUniversity of Delaware · US

Funding

Design and Utility of Novel Protienaceous BiomaterialsZIABC011313 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$19.0M
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
6 · The paper itself

Abstract

Hydrogels prepared from self-assembling peptides are promising materials for medical applications, and using both l- and d-peptide isomers in a gel's formulation provides an intuitive way to control the proteolytic degradation of an implanted material. In the course of developing gels for delivery applications, we discovered that a racemic mixture of the mirror-image β-hairpin peptides, named MAX1 and DMAX1, provides a fibrillar hydrogel that is four times more rigid than gels formed by either peptide alone-a puzzling observation. Herein, we use transmission electron microscopy, small angle neutron scattering, solid state NMR, diffusing wave, infrared, and fluorescence spectroscopies, and modeling to determine the molecular basis for the increased mechanical rigidity of the racemic gel. We find that enantiomeric peptides coassemble in an alternating fashion along the fibril long axis, forming an extended heterochiral pleat-like β-sheet, a structure predicted by Pauling and Corey in 1953. Hydrogen bonding between enantiomers within the sheet dictates the placement of hydrophobic valine side chains in the fibrils' dry interior in a manner that allows the formation of nested hydrophobic interactions between enantiomers, interactions not accessible within enantiomerically pure fibrils. Importantly, this unique molecular arrangement of valine side chains maximizes inter-residue contacts within the core of the fibrils resulting in their local stiffening, which in turn, gives rise to the significant increase in bulk mechanical rigidity observed for the racemic hydrogel.

Identifiers

PMID28691070
PMCPMC5492410
OpenAlexW2619102628

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.