Evidence map›Paper›PMID 36438597›Full record

ArticleMacromolecules2022

Noncovalent Enzyme Nanogels via a Photocleavable Linkage.

Neil L Forsythe, Mikayla F Tan, Daniele Vinciguerra, Jacquelin Woodford, Adam Z Stieg, Heather D Maynard

Open access · hybridAbstract read
In one paragraph

Article in Macromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. 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

6 authors at 1 institution in 1 country.

Neil L ForsytheDepartment of Chemistry and Biochemistry, University of California, 607 Charles E. Young Drive East, Los Angeles, California 90095, United States.
Mikayla F TanDepartment of Chemistry and Biochemistry, University of California, 607 Charles E. Young Drive East, Los Angeles, California 90095, United States.
Daniele VinciguerraCalifornia NanoSystems Institute, 570 Westwood Plaza Building 114, Los Angeles, California 90095, United States.ORCID https://orcid.org/0000-0003-0755-2951
Jacquelin WoodfordDepartment of Chemistry and Biochemistry, University of California, 607 Charles E. Young Drive East, Los Angeles, California 90095, United States.
Adam Z StiegCalifornia NanoSystems Institute, 570 Westwood Plaza Building 114, Los Angeles, California 90095, United States.
Heather D MaynardDepartment of Chemistry and Biochemistry, University of California, 607 Charles E. Young Drive East, Los Angeles, California 90095, United States.ORCID https://orcid.org/0000-0003-3692-6289
California NanoSystems Institute · US

Funding

CHEMISTRY BIOLOGY INTERFACE TRAINING PROGRAMT32GM008496 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 1993 to 2019
$6.3M
Stable and Active bFGF-Polymer Conjugates for Wound HealingR01EB013674 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 2012 to 2015
$1.3M
Trehalose Glycopolymers to Enhance both Pharmacokinetics and Stability of Therapeutic ProteinsR01EB020676 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 2016 to 2019
$1.3M
Stabilization of Glucagon by Trehalose Gylcopolymer NanogelsR01DK127908 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 2021 to 2023
$1.1M
NIBIB NIH HHS R01 EB013674NIBIB NIH HHS R01 EB020676NIDDK NIH HHS R01 DK127908NIGMS NIH HHS T32 GM008496
6 · The paper itself

Abstract

Enzyme nanogels (ENGs) offer a convenient method to protect therapeutic proteins from in vivo stressors. Current methodologies to prepare ENGs rely on either covalent modification of surface residues or the noncovalent assembly of monomers at the protein surface. In this study, we report a new method for the preparation of noncovalent ENGs that utilizes a heterobifunctional, photocleavable monomer as a hybrid approach. Initial covalent modification with this monomer established a polymerizable handle at the protein surface, followed by radical polymerization with poly(ethylene glycol) methacrylate monomer and ethylene glycol dimethacrylate crosslinker in solution. Final photoirradiation cleaved the linkage between the polymer and protein to afford the noncovalent ENGs. The enzyme phenylalanine ammonia lyase (PAL) was utilized as a model protein yielding well-defined nanogels 80 nm in size by dynamic light scattering (DLS) and 76 nm by atomic force microscopy. The stability of PAL after exposure to trypsin or low pH was assessed and was found to be more stable in the noncovalent nanogel compared to PAL alone. This approach may be useful for the stabilization of active enzymes.

Identifiers

PMID36438597
PMCPMC9686129
OpenAlexW4308483458

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.