Evidence map›Paper›PMID 34606089›Full record

ArticleBiotechnology and bioengineering2021

Stability of proteins encapsulated in Michael-type addition polyethylene glycol hydrogels.

Zahra Ghassemi, Samuel Ruesing, Jennie B Leach, Silviya P Zustiak

Open access · greenAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Toward Bioactive Hydrogels: A Tunable Approach via Nucleic Acid-Collagen Complexation.Regenerative engineering and translational medicine · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. 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

4 authors at 2 institutions in 1 country.

Zahra GhassemiDepartment of Chemical, Biochemical, and Environmental Engineering, University of Maryland, Baltimore, Maryland, USA.
Samuel RuesingDepartment of Biomedical Engineering, Saint Louis University, St. Louis, Missouri, USA.
Jennie B LeachDepartment of Chemical, Biochemical, and Environmental Engineering, University of Maryland, Baltimore, Maryland, USA.
Silviya P ZustiakDepartment of Biomedical Engineering, Saint Louis University, St. Louis, Missouri, USA.ORCID 0000-0002-7648-8351
Saint Louis University · USUniversity of Maryland, Baltimore · US

Funding

EXPAND PARTICIPATION BY MINORITIES IN BIOMEDICAL SCIENCER25GM055036 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1996 to 2021
$16.9M
Aptamer-Hydrogel Hybrid Sensors for Continuous Therapeutic Drug MonitoringR01GM117159 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI WHITE, RYAN J. · 2016 to 2020
$1.2M
NIGMS NIH HHS R01 GM117159NIGMS NIH HHS R25 GM055036
6 · The paper itself

Abstract

Degradable polyethylene glycol (PEG) hydrogels are excellent vehicles for sustained drug release due to their biocompatibility, tunable physical properties, and customizable degradation. However, protein therapeutics are unstable under physiological conditions and releasing degraded or inactive therapeutics can induce immunogenic effects. While controlling protein release from PEG hydrogels has been extensively investigated, few studies have detailed protein stability long-term or under stress conditions. Here, lysozyme and alcohol dehydrogenase (ADH) stability were explored upon encapsulation in PEG hydrogels formed through Michael-type addition. The stability and structure of the two model proteins were monitored by measuring the free energy of unfolding and fluoresce quenching when confined in a hydrogel and compared to PEG solution and buffer. Hydrogels destabilized lysozyme structure at low denaturant concentrations but prevented complete unfolding at high concentrations. ADH was stabilized as the confining mesh size approached the protein radius of gyration. Both proteins retained enzymatic activity within the hydrogels under stress conditions, including denaturant, high temperature, and agitation. Conjugation between lysozyme and PEG-acrylate was identified at long reaction times but no conjugation was observed in the time required for complete gelation. Studies of protein stability in PEG hydrogels, as the one detailed here, can lead to designer technologies for the improved formulation, storage, and delivery of protein therapeutics.

Indexed as

Biocompatible MaterialsDrug CompoundingHydrogelsPolyethylene GlycolsProteinsProtein StabilityProtein UnfoldingThermodynamicsBiocompatible MaterialsHydrogelsPolyethylene GlycolsProteinsconfinementdrug deliveryhydrogelspoly(ethylene) glycolprotein stability

Identifiers

PMID34606089
PMCPMC8585711
OpenAlexW3202216803

What OpenQuestion holds

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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.