Evidence map›Paper›PMID 39676522›Full record

ArticleMacromolecular rapid communications2025

Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH-Dependent Assembly.

Norbert Osiński, Karolina Majsterkiewicz, Zuzanna Pakosz-Stępień, Yusuke Azuma, Artur P Biela, Szymon Gaweł, Jonathan G Heddle

Abstract read
In one paragraph

Article in Macromolecular rapid communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

7 authors.

Norbert OsińskiMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0000-0002-3340-0129
Karolina MajsterkiewiczMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0000-0001-9734-1837
Zuzanna Pakosz-StępieńSchool of Biological and Biomedical Sciences, Durham University, Durham, DH1-3LE, UK.ORCID https://orcid.org/0000-0002-2288-8616
Yusuke AzumaMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0000-0003-3543-3159
Artur P BielaMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0000-0001-6733-242X
Szymon GawełMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0009-0009-3228-542X
Jonathan G HeddleMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków, 30387, Poland.ORCID https://orcid.org/0000-0003-0994-9928

Funding

Foundation for Polish Science)Laboratory for Analytical Atomic Spectrometry, Jagiellonian UniversityLeverhulme Trust LIP-2022-010MCB Structural Biology Core FacilityNarodowe Centrum Nauki 2016/20/W/NZ1/00095Polish National Science Centre 2019/34/A/NZ1/00196Priority Research Area under the Strategic Programme Excellence Initiative at Jagiellonian University
6 · The paper itself

Abstract

The rational design and production of a novel series of engineered protein cages are presented, which have emerged as versatile and adaptable platforms with significant applications in biomedicine. These protein cages are assembled from multiple protein subunits, and precise control over their interactions is crucial for regulating assembly and disassembly, such as the on-demand release of encapsulated therapeutic agents. This approach employs a homo-undecameric, ring-shaped protein scaffold with strategically positioned metal binding sites. These engineered proteins can self-assemble into highly stable cages in the presence of cobalt or zinc ions. Furthermore, the cages can be disassembled on demand by employing external triggers such as chelating agents and changes in pH. Interestingly, for certain triggers, the disassembly process is reversible, allowing the cages to reassemble upon reversal or outcompeting of triggering conditions/agents. This work offers a promising platform for the development of advanced drug delivery systems and other biomedical applications.

Indexed as

CobaltProteinsZincHydrogen-Ion ConcentrationProtein EngineeringCobaltProteinsZinc

Identifiers

PMID39676522
PMCPMC11925324

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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.