ArticlePloS one2014
Function, structure, and stability of enzymes confined in agarose gels.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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.
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.
Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
- Encapsulation of Active Substances in Natural Polymer Coatings.Materials (Basel, Switzerland) · 2024Review
- Role of Polymer Concentration on the Release Rates of Proteins from Single- and Double-Network Hydrogels.International journal of molecular sciences · 2023Article
- The Effect of Gelatin Source on the Synthesis of Gelatin-Methacryloyl and the Production of Hydrogel Microparticles.Gels (Basel, Switzerland) · 2023Article
- Single-tube collection and nucleic acid analysis of clinical samples for SARS-CoV-2 saliva testing.Scientific reports · 2022Article
- Investigation of Lysozyme Diffusion in Agarose Hydrogels Employing a Microfluidics-Based UV Imaging Approach.Frontiers in bioengineering and biotechnology · 2022Article
- Stability of proteins encapsulated in Michael-type addition polyethylene glycol hydrogels.Biotechnology and bioengineering · 2021Article
- Review
- Combined Effects of Confinement and Macromolecular Crowding on Protein Stability.International journal of molecular sciences · 2020Article
- Biodegradable polyethylene glycol hydrogels for sustained release and enhanced stability of rhGALNS enzyme.Drug delivery and translational research · 2020Article
- Silk fibroin hydrogels from the Colombian silkworm Bombyx mori L: Evaluation of physicochemical properties.PloS one · 2019Article
- Effective detection of biocatalysts with specified activity by using a hydrogel-based colourimetric assay - β-galactosidase case study.PloS one · 2018Article
- Enzymatic reactions in confined environments.Nature nanotechnology · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Research over the past few decades has attempted to answer how proteins behave in molecularly confined or crowded environments when compared to dilute buffer solutions. This information is vital to understanding in vivo protein behavior, as the average spacing between macromolecules in the cell cytosol is much smaller than the size of the macromolecules themselves. In our study, we attempt to address this question using three structurally and functionally different model enzymes encapsulated in agarose gels of different porosities. Our studies reveal that under standard buffer conditions, the initial reaction rates of the agarose-encapsulated enzymes are lower than that of the solution phase enzymes. However, the encapsulated enzymes retain a higher percentage of their activity in the presence of denaturants. Moreover, the concentration of agarose used for encapsulation had a significant effect on the enzyme functional stability; enzymes encapsulated in higher percentages of agarose were more stable than the enzymes encapsulated in lower percentages of agarose. Similar results were observed through structural measurements of enzyme denaturation using an 8-anilinonaphthalene-1-sulfonic acid fluorescence assay. Our work demonstrates the utility of hydrogels to study protein behavior in highly confined environments similar to those present in vivo; furthermore, the enhanced stability of gel-encapsulated enzymes may find use in the delivery of therapeutic proteins, as well as the design of novel strategies for biohybrid medical devices.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.