Evidence map›Paper›PMID 31784506›Full record

ArticleNature communications2019

Chemical unfolding of protein domains induces shape change in programmed protein hydrogels.

Luai R Khoury, Ionel Popa

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Fully Reshapeable and Recyclable Protein Hydrogels.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  6. Review
  7. Article
  8. Plasmonic Single-Molecule Affinity Detection at 10Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  9. Review
  10. Capturing Dynamic Assembly of Nanoscale Proteins During Network Formation.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  11. Strain learning in protein-based mechanical metamaterials.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Toward Tunable Protein-Driven Hydrogel Lens.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  18. Review
  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

2 authors at 1 institution in 1 country.

Luai R KhouryDepartment of Physics, University of Wisconsin-Milwaukee, 3135 North Maryland Ave., Milwaukee, WI, 53211, USA. khoury@uwm.edu.
Ionel PopaDepartment of Physics, University of Wisconsin-Milwaukee, 3135 North Maryland Ave., Milwaukee, WI, 53211, USA. popa@uwm.edu.ORCID http://orcid.org/0000-0003-3111-4716
University of Wisconsin–Milwaukee · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffness of protein-based hydrogels made from bovine serum albumin (BSA) by using polyelectrolytes such as polyethyleneimine (PEI) and poly-L-lysine (PLL) at various concentrations. This approach confers protein-hydrogels with tunable wide-range stiffness, from ~10-64 kPa, without affecting the protein mechanics and nanostructure. We use the 6-fold increase in stiffness induced by PEI to program BSA hydrogels in various shapes. By utilizing the characteristic protein unfolding we can induce reversible shape-memory behavior of these composite materials using chemical denaturing solutions. The approach demonstrated here, based on protein engineering and polymer reinforcing, may enable the development and investigation of smart biomaterials and extend protein hydrogel capabilities beyond their conventional applications.

Indexed as

Biocompatible MaterialsNanostructuresProtein UnfoldingAnimalsBiomechanical PhenomenaCattleElasticityHydrogelsPolyethyleneiminePolylysineSerum Albumin, BovineBiocompatible MaterialsHydrogelsPolyethyleneiminePolylysineSerum Albumin, Bovine

Identifiers

PMID31784506
PMCPMC6884551
OpenAlexW2991434999

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.