Evidence map›Paper›PMID 40499751›Full record

ArticleJournal of advanced research2026

Construction of mitochondrial-targeted ferritin carrier: subunit-terminal fused mitochondrial presequences facilitate efficient delivery.

Jia Zeng, Yitong Li, Xinning Fang, Han Yu, Mengyuan Xu, Xiangyu Zhao, Zhenghong Wu, Xiaole Qi

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PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of advanced research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed.

  1. 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

8 authors.

Jia ZengKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Yitong LiKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Xinning FangKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Han YuKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Mengyuan XuKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Xiangyu ZhaoKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China.
Zhenghong WuKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China. Electronic address: zhenghongwu66@cpu.edu.cn.
Xiaole QiKey Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China; Industrial Technology Innovation Platform, Zhejiang Center for Safety Study of Drug Substances, Hangzhou 310018, China. Electronic address: qixiaole523@cpu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionProtein sorting within mitochondria is intricately linked to the amino acid sequence facilitating the transmembrane transport of proteins into this organelle. Leveraging the Mitochondrial Targeting Signal (MTS)-mediated protein sorting mechanism presents a promising strategy for directing therapeutic agents into the mitochondria.

objectivesBy fusing MTS to the subunit terminus of recombinant heavy chain ferritin (HFn), we aim to establish a highly effective mitochondrial targeting vector. This fusion is designed to enhance the ability to specifically direct and accumulate within mitochondria, and to precisely deliver Lonidamine (LND), a selective metabolic inhibitor, into these organelles, ultimately realizing potent anti-tumor activity.

methodsUtilizing gene engineering strategies, a plasmid encoding MTS-modified HFn (MTS-HFn) was transferred into E.coli to induce protein expression. At the cellular level, the mitochondrial targeting capacity of MTS-HFn was investigated. Subsequently, LND was encapsulated within MTS-HFn, and its tumoral accumulation and anti-tumor efficacy were studied in tumor-bearing models.

resultsMTS-HFn demonstrated exceptional mitochondrial targeting, achieving a 2.7-fold higher accumulation in mitochondria compared to wild-type HFn. The targeting mechanism exploration unveiled that the positive charge of MTS drives aggregation of HFn around mitochondria, and mediates its entry into the mitochondrial matrix via the TOM/TIM complex. In vivo antitumor activity studies revealed that MTS-HFn preserved its inherent tumor targeting ability and significantly enhanced the tumor suppressive effect of LND, yielding an inhibition rate of 51.06%.

conclusionThis vector inspired by natural mitochondrial protein sorting represents an optimal hierarchical delivery system for targeting both tumor and mitochondrial, offering a dependable alternative for precise treatment strategies in mitochondrial diseases.

Indexed as

FerritinsMitochondriaAnimalsCell Line, TumorDrug Delivery SystemsHumansMiceProtein TransportRecombinant Fusion ProteinsXenograft Model Antitumor AssaysFerritinsRecombinant Fusion ProteinsHierarchical deliveryHuman ferritin nanocageMitochondrial targeting signalMitochondria targeting

Identifiers

PMID40499751
PMCPMC12957843

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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.