ArticleBiosensors2021
Mechanism Study of Thermally Induced Anti-Tumor Drug Loading to Engineered Human Heavy-Chain Ferritin Nanocages Aided by Computational Analysis.
Article in Biosensors, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Tryptophan Residues' Incorporation Modulates Ferritin Thermal Stability and Hydrophobicity.Current issues in molecular biology · 2026Article
- A tumor-targeting black phosphorus-based nanoplatform for controlled chemo-photothermal therapy of breast cancer.Materials today. Bio · 2025Article
- Novel engineered HER2 specific recombinant protein nanocages for targeted drug delivery.Molecular biology reports · 2024Article
- Ferritin in cancer therapy: A pleiotropic tumoraffin nanocage-based transport.Cancer medicine · 2023Review
- Nanoprobes for Tumor Theranostics.Biosensors · 2022Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
Diverse drug loading approaches for human heavy-chain ferritin (HFn), a promising drug nanocarrier, have been established. However, anti-tumor drug loading ratio and protein carrier recovery yield are bottlenecks for future clinical application. Mechanisms behind drug loading have not been elaborated. In this work, a thermally induced drug loading approach was introduced to load anti-tumor drug doxorubicin hydrochloride (DOX) into HFn, and 2 functionalized HFns, HFn-PAS-RGDK, and HFn-PAS. Optimal conditions were obtained through orthogonal tests. All 3 HFn-based proteins achieved high protein recovery yield and drug loading ratio. Size exclusion chromatography (SEC) and transmission electron microscopy (TEM) results showed the majority of DOX loaded protein (protein/DOX) remained its nanocage conformation. Computational analysis, molecular docking followed by molecular dynamic (MD) simulation, revealed mechanisms of DOX loading and formation of by-product by investigating non-covalent interactions between DOX with HFn subunit and possible binding modes of DOX and HFn after drug loading. In in vitro tests, DOX in protein/DOX entered tumor cell nucleus and inhibited tumor cell growth.
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Registered trials
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