Evidence map›Paper›PMID 32263077›Full record

ArticleJournal of materials chemistry. B2016

Protein release from highly charged peptide hydrogel networks.

Katelyn Nagy-Smith, Yuji Yamada, Joel P Schneider

Abstract read
In one paragraph

Article in Journal of materials chemistry. B, 2016. 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
–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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies.Journal of peptide science : an official publication of the European Peptide Society · 2022
    Review
  9. Review
  10. Review
  11. Tunable Protein Hydrogels: Present State and Emerging Development.Advances in biochemical engineering/biotechnology · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Peptide Tectonics: Encoded Structural Complementarity Dictates Programmable Self-Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  18. Article
  19. Article
  20. Article
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

3 authors.

Katelyn Nagy-SmithChemical Biology Laboratory, National Cancer Institute, Frederick, MD 21702, USA. Joel.Schneider@nih.gov.
Yuji Yamada
Joel P Schneider

Funding

Design and Utility of Novel Protienaceous BiomaterialsZIABC011313 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$19.0M
Protein Assembly in Materials, Biology and Medicine:Direct Impact on Biological NR13DE018358 · NIDCR · UNIVERSITY OF DELAWARE · PI SCHNEIDER, JOEL P · 2007 to 2007
$18k
Intramural NIH HHS ZIA BC011313NIDCR NIH HHS R13 DE018358
6 · The paper itself

Abstract

Hydrogels are useful delivery vehicles for therapeutic proteins. The ability to control the rate of protein release is paramount to a gel's utility and, in part, defines its clinical application. Electrostatic interactions made between encapsulated protein and a gel's network represents one modality in which protein motility can be controlled. For many gels this strategy works well under low ionic strength solution conditions, but dramatically less so in solutions of physiologically relevant ionic strength where electrostatic interactions are more effectively screened. Herein, we find that highly charged self-assembling peptides can be used to prepare fibrillar hydrogels of sufficient electropotential to allow electrostatic-based control over protein release under physiological buffer conditions. Rheology shows that proteins, differing significantly in their isoelectric point, can be directly encapsulated within negatively- or positively-charged peptide hydrogel networks during the peptide self-assembly event leading to gelation. Bulk adsorption studies coupled with transmission electron microscopy shows that electrostatic interactions drive the association of protein to oppositely charged fibrils in the final gel state, which in turn, dictates the diffusion and retention of these macromolecules in the hydrogel network.

Identifiers

PMID32263077
PMCPMC8244587

What OpenQuestion holds

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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.