Evidence map›Paper›PMID 33026394›Full record

ArticleJournal of materials chemistry. B2020

Tuneable peptide cross-linked nanogels for enzyme-triggered protein delivery.

Lucia Massi, Adrian Najer, Robert Chapman, Christopher D Spicer, Valeria Nele, Junyi Che, Marsilea A Booth, James J Doutch, Molly M Stevens

Open access · hybridAbstract read
In one paragraph

Article in Journal of materials chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Stimuli-responsive polypeptide nanogels for trypsin inhibition.Beilstein journal of nanotechnology · 2022
    Article
  13. Review
  14. Review
  15. Review
  16. Nanogels Capable of Triggered Release.Advances in biochemical engineering/biotechnology · 2021
    Review
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

9 authors at 3 institutions in 2 countries.

Lucia MassiDepartment of Materials, Department of Bioengineering, and Institute of Biomedical Engineering, Imperial College London, London SW7 2AZ, UK. m.stevens@imperial.ac.uk.
Adrian Najer
Robert Chapman
Christopher D Spicer
Valeria Nele
Junyi Che
Marsilea A Booth
James J Doutch
Molly M Stevens
Imperial College London · GBRutherford Appleton Laboratory · GBUNSW Sydney · AU

Funding

British Heart Foundation RM/13/1/30157Medical Research Council MR/K026682/1Medical Research Council MR/R015651/1Wellcome Trust 098411Wellcome Trust 098411/Z/12/ZWellcome Trust 209121Wellcome Trust 209121/Z/17/ZWellcome Trust 209121_Z_17_Z
6 · The paper itself

Abstract

Many diseases are associated with the dysregulated activity of enzymes, such as matrix metalloproteinases (MMPs). This dysregulation can be leveraged in drug delivery to achieve disease- or site-specific cargo release. Self-assembled polymeric nanoparticles are versatile drug carrier materials due to the accessible diversity of polymer chemistry. However, efficient loading of sensitive cargo, such as proteins, and introducing functional enzyme-responsive behaviour remain challenging. Herein, peptide-crosslinked, temperature-sensitive nanogels for protein delivery were designed to respond to MMP-7, which is overexpressed in many pathologies including cancer and inflammatory diseases. The incorporation of N-cyclopropylacrylamide (NCPAM) into N-isopropylacrylamide (NIPAM)-based copolymers enabled us to tune the polymer lower critical solution temperature from 33 to 44 °C, allowing the encapsulation of protein cargo and nanogel-crosslinking at slightly elevated temperatures. This approach resulted in nanogels that were held together by MMP-sensitive peptides for enzyme-specific protein delivery. We employed a combination of cryogenic transmission electron microscopy (cryo-TEM), dynamic light scattering (DLS), small angle neutron scattering (SANS), and fluorescence correlation spectroscopy (FCS) to precisely decipher the morphology, self-assembly mechanism, enzyme-responsiveness, and model protein loading/release properties of our nanogel platform. Simple variation of the peptide linker sequence and combining multiple different crosslinkers will enable us to adjust our platform to target specific diseases in the future.

Indexed as

Acrylic ResinsAnimalsCattleDrug CarriersDrug LiberationMatrix Metalloproteinase 7MiceNanogelsPeptidesRAW 264.7 CellsSerum Albumin, BovineAcrylic ResinsDrug CarriersMatrix Metalloproteinase 7NanogelsPeptidesSerum Albumin, Bovine

Identifiers

PMID33026394
PMCPMC7613372
OpenAlexW3083341292

What OpenQuestion holds

Textmetadata
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.