Evidence map›Paper›PMID 37883077›Full record

ArticleProtein science : a publication of the Protein Society2023

Hydrophobicity-enhanced ferritin nanoparticles for efficient encapsulation and targeted delivery of hydrophobic drugs to tumor cells.

Alessio Incocciati, Jan Kubeš, Roberta Piacentini, Chiara Cappelletti, Sofia Botta, Lucia Bertuccini, Tomáš Šimůnek, Alberto Boffi, Alberto Macone, Alessandra Bonamore

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

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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

10 authors at 4 institutions in 2 countries.

Alessio IncocciatiDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.ORCID 0000-0003-2982-8592
Jan KubešDepartment of Biochemical Sciences, Faculty of Pharmacy in Hradec Králové, Charles University, Hradec Králové, Czech Republic.
Roberta PiacentiniDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Chiara CappellettiDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Sofia BottaDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Lucia BertucciniCore Facilities, Istituto Superiore di Sanità, Rome, Italy.
Tomáš ŠimůnekDepartment of Biochemical Sciences, Faculty of Pharmacy in Hradec Králové, Charles University, Hradec Králové, Czech Republic.
Alberto BoffiDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Alberto MaconeDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.ORCID 0000-0003-0455-1400
Alessandra BonamoreDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Sapienza University of Rome · ITCharles University · CZIstituto Superiore di Sanità · ITItalian Institute of Technology · IT

Funding

Charles University SVV260664NextGenerationEU PNRR M4C2-Investimento 1.4-CN00000041Sapienza University of Rome, SEED-PNR 2022 SP1221846100319C
6 · The paper itself

Abstract

Ferritin, a naturally occurring iron storage protein, has gained significant attention as a drug delivery platform due to its inherent biocompatibility and capacity to encapsulate therapeutic agents. In this study, we successfully genetically engineered human H ferritin by incorporating 4 or 6 tryptophan residues per subunit, strategically oriented towards the inner cavity of the nanoparticle. This modification aimed to enhance the encapsulation of hydrophobic drugs into the ferritin cage. Comprehensive characterization of the mutants revealed that only the variant carrying four tryptophan substitutions per subunit retained the ability to disassemble and reassemble properly. As a proof of concept, we evaluated the loading capacity of this mutant with ellipticine, a natural hydrophobic indole alkaloid with multimodal anticancer activity. Our data demonstrated that this specific mutant exhibited significantly higher efficiency in loading ellipticine compared to human H ferritin. Furthermore, to evaluate the versatility of this hydrophobicity-enhanced ferritin nanoparticle as a drug carrier, we conducted a comparative study by also encapsulating doxorubicin, a commonly used anticancer drug. Subsequently, we tested both ellipticine and doxorubicin-loaded nanoparticles on a promyelocytic leukemia cell line, demonstrating efficient uptake by these cells and resulting in the expected cytotoxic effect.

Indexed as

Antineoplastic AgentsEllipticinesNanoparticlesApoferritinsCell Line, TumorDoxorubicinDrug CarriersDrug Delivery SystemsFerritinsHumansHydrophobic and Hydrophilic InteractionsTryptophanAntineoplastic AgentsApoferritinsDoxorubicinDrug CarriersEllipticinesFerritinsTryptophandoxorubicindrug deliveryellipticineferritinhydrophobic drugsnanoparticleprotein engineeringtumor cells

Identifiers

PMID37883077
PMCPMC10661074
OpenAlexW4387950625

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.