Evidence map›Paper›PMID 28365480›Full record

ArticleActa biomaterialia2017

Rational design of charged peptides that self-assemble into robust nanofibers as immune-functional scaffolds.

Hangyu Zhang, Jaehyung Park, Yonghou Jiang, Kim A Woodrow

Abstract read
In one paragraph

Article in Acta biomaterialia, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Peptide-Based Drug Delivery Systems.Medicina (Kaunas, Lithuania) · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Self-Assembling Peptide-Based Hydrogels in Angiogenesis.International journal of nanomedicine · 2020
    Review
  17. Article
  18. Self-Assembling Peptides and Their Application in the Treatment of Diseases.International journal of molecular sciences · 2019
    Review
  19. Article
  20. Bionanotechnology for vaccine design.Current opinion in biotechnology · 2018
    Review
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 at 1 institution in 1 country.

Hangyu ZhangDepartment of Bioengineering, University of Washington, Foege N410D, 3720 15th Ave NE, Seattle, WA 98195-5061, USA.
Jaehyung ParkDepartment of Bioengineering, University of Washington, Foege N410D, 3720 15th Ave NE, Seattle, WA 98195-5061, USA.
Yonghou JiangDepartment of Bioengineering, University of Washington, Foege N410D, 3720 15th Ave NE, Seattle, WA 98195-5061, USA.
Kim A WoodrowDepartment of Bioengineering, University of Washington, Foege N410D, 3720 15th Ave NE, Seattle, WA 98195-5061, USA. Electronic address: woodrow@uw.edu.
University of Washington · US

Funding

Nanomaterials for engineering protection in the genital mucosaDP2HD075703 · NICHD · UNIVERSITY OF WASHINGTON · PI WOODROW, KIM A. · 2012 to 2012
$2.3M
NICHD NIH HHS DP2 HD075703
6 · The paper itself

Abstract

Self-assembling peptides programed by sequence design to form predefined nanostructures are useful for a variety of biomedical applications. However, assemblies of classic ionic self-complementary peptides are unstable in neutral pH, while charged peptide hydrogels have low mechanical strength. Here, we report on the rational design of a self-assembling peptide system with optimized charge distribution and density for bioscaffold development. Our designer peptides employs a sequence pattern that undergoes salt triggered self-assembly into β-sheet rich cationic nanofibers in the full pH range (pH 0-14). Our peptides form nanofibrils in physiological condition at a minimum concentration that is significantly lower than has been reported for self-assembly of comparable peptides. The robust fiber-forming ability of our peptides results in the rapid formation of hydrogels in physiological conditions with strong mechanical strength. Moreover, fiber structure is maintained even upon dense conjugation with a model bioactive cargo OVA STATEMENT OF SIGNIFICANCE: This work is an attempt of rational design of materials from molecular level for targeted properties and an exploration in molecular self-assembly. Current widely studied self-assembling peptides do not have stable nanofiber structures and form weak hydrogels under physiological conditions. To address this issue, we develop charged self-assembling peptides with a novel sequence pattern for strong fiber-forming ability under physiological conditions. Our designer peptides can undergo salt-triggered self-assembly into nanofibers that are ultrastable in extreme pH (0-14) and dilute solutions, and into hydrogels with strong mechanical strength. Upon conjugation with a model bioactive cargo, our self-assembled peptides exhibit great potential as bioscaffolds for multiple applications.

Indexed as

HydrogelsHydrogen-Ion ConcentrationNanofibersPeptidesTissue ScaffoldsHydrogelsPeptidesHydrogelNanofiberPeptideScaffoldSelf-assembly

Identifiers

PMID28365480
PMCPMC5578403
OpenAlexW2601440627

What OpenQuestion holds

Textmetadata
LicenceTDM
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.