Evidence map›Paper›PMID 38228804›Full record

ArticleNature nanotechnology2024

Controlled adsorption of multiple bioactive proteins enables targeted mast cell nanotherapy.

Fanfan Du, Clayton H Rische, Yang Li, Michael P Vincent, Rebecca A Krier-Burris, Yuan Qian, Simseok A Yuk, Sultan Almunif, Bruce S Bochner, Baofu Qiao and 1 more

Abstract read
In one paragraph

Article in Nature nanotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Siglecs: From Biomodulation to Immunotherapy.Current protein & peptide science · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Fanfan Du *Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA.ORCID 0000-0001-5374-4087
Clayton H Rische *Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA.ORCID 0000-0003-3610-2116
Yang Li *Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-6286-0052
Michael P VincentDepartment of Biomedical Engineering, Northwestern University, Evanston, IL, USA.
Rebecca A Krier-BurrisDepartment of Medicine, Division of Allergy and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0001-9722-215X
Yuan QianDepartment of Biomedical Engineering, Northwestern University, Evanston, IL, USA.
Simseok A YukDepartment of Biomedical Engineering, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-6610-4940
Sultan AlmunifDepartment of Biomedical Engineering, Northwestern University, Evanston, IL, USA.
Bruce S BochnerDepartment of Medicine, Division of Allergy and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0002-9411-6009
Baofu QiaoDepartment of Materials Science and Engineering, Northwestern University, Evanston, IL, USA.ORCID 0000-0001-8870-5985
Evan A ScottDepartment of Biomedical Engineering, Northwestern University, Evanston, IL, USA. evan.scott@northwestern.edu.ORCID 0000-0002-8945-2892

Funding

Using siglecs and their ligands to treat allergic diseases SALTADU19AI136443 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BOCHNER, BRUCE S · 2018 to 2022
$7.6M
A universal multi-drug encapsulation and delivery system employing supramolecular nanogels that self-assemble via dynamic sulfone bondingR01EB030629 · NIBIB · NORTHWESTERN UNIVERSITY · PI SCOTT, EVAN ALEXANDER · 2021 to 2024
$1.8M
Exploiting Siglec-6 for targeted anti-allergy drug delivery into human mast cellsR21AI159586 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BOCHNER, BRUCE S, SCOTT, EVAN ALEXANDER · 2021 to 2022
$417k
National Science Foundation (NSF) DMR-0520547NIAID NIH HHS R21 AI159586NIAID NIH HHS U19 AI136443NIBIB NIH HHS R01 EB030629NSF DMR-1720139NSF ECCS-2025633
6 · The paper itself

Abstract

Protein adsorption onto nanomaterials often results in denaturation and loss of bioactivity. Controlling the adsorption process to maintain the protein structure and function has potential for a range of applications. Here we report that self-assembled poly(propylene sulfone) (PPSU) nanoparticles support the controlled formation of multicomponent enzyme and antibody coatings and maintain their bioactivity. Simulations indicate that hydrophobic patches on protein surfaces induce a site-specific dipole relaxation of PPSU assemblies to non-covalently anchor the proteins without disrupting the protein hydrogen bonding or structure. As a proof of concept, a nanotherapy employing multiple mast-cell-targeted antibodies for preventing anaphylaxis is demonstrated in a humanized mouse model. PPSU nanoparticles displaying an optimized ratio of co-adsorbed anti-Siglec-6 and anti-FcεRIα antibodies effectively inhibit mast cell activation and degranulation, preventing anaphylaxis. Protein immobilization on PPSU surfaces provides a simple and rapid platform for the development of targeted protein nanomedicines.

Indexed as

Mast CellsNanoparticlesAdsorptionAnaphylaxisAnimalsCell DegranulationHumansMiceNanomedicinePolypropylenesPolypropylenes

Identifiers

PMID38228804
PMCPMC11105988

What OpenQuestion holds

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Registered trials

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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.