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Glycation of ferritin provides a viable approach to enhance its physicochemical and functional properties. However, there is limited research on the interfacial adsorption properties of glycated ferritin-based colloidal particles. Therefore, this study selected recombinant human H-chain ferritin (rHuHF), rHuHF encapsulated with resveratrol (rHuHF-Res), and rHuHF-dextran glycoconjugates loaded with resveratrol (Dex-rHuHF-Res) as emulsifiers to investigate their interfacial adsorption properties.

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Article Synopsis
  • Monocytes and macrophages are critical for defending the body but also play a role in inflammation-related diseases, complicating their study.
  • Researchers identified the Fth1 gene, linked to ferritin H chain production, as a key indicator of alveolar macrophage activity during lung inflammation, using a specialized Fth1-mScarlet reporter mouse to monitor this process.
  • The Fth1 marker showed increased activity in monocytes during inflammation and helped distinguish between different immune cell types, potentially improving our understanding of macrophage responses and differentiation in inflammatory conditions.
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Construction of robust protein nanocage by designed disulfide bonds for active cargo molecules protection in the gastric environment.

J Colloid Interface Sci

January 2025

State Key Laboratory of Food Nutrition and Safety and School of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address:

Notwithstanding the progress made, cargo molecules encapsulated within ferritin via oral administration in the gastric environment remains a persistent challenge. This study focuses on the strategic enhancement of ferritin stability in harsh gastric environment. By taking advantagie of computational-assisted design, we strategically introduced up to 96 disulfide bonds along three key inter-subunit interfaces to one single ferritin molecule with human H-chain ferritin and shrimp (Marsupenaeus japonicus) ferritin as starting materials, producing two kinds of robust ferritin nanocages with markedly enhanced acid and protease (pepsin and rennin) resistance.

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Hydroxychloroquine loaded hollow apoferritin nanocages for cancer drug repurposing and autophagy inhibition.

Eur J Pharm Biopharm

October 2024

Key Laboratory of Modern Chinese Medicines, China Pharmaceutical University, Nanjing 210009, China; Hangzhou Innovative Institute of Pharmaceutics, China Pharmaceutical University, Hangzhou 310018, China. Electronic address:

Hydroxychloroquine sulfate (HCQ) is currently being repurposed for cancer treatment. The antitumor mechanism of HCQ is inhibition of cellular autophagy, but its therapeutic potential is severely limited by poor solubility, lack of tumor targeting and lower cellular uptake. Therefore, utilization of human H-chain apoferritin (HFn) composed only of heavy subunits is an attractive approach for tumor targeting drug delivery.

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Ferritins are natural proteins which spontaneously self-assemble forming hollow nanocages physiologically deputed to iron storage and homeostasis. Thanks to their high stability and easy production in vitro, ferritins represent an intriguing system for nanobiotechnology. Here we investigated the mechanism of disassembly and reassembly of a human recombinant ferritin constituted by the heavy chain (hHFt) exploiting a new procedure which involves the use of minimal amounts of sodium dodecyl sulfate (SDS) and assessed its effectiveness in comparison with two commonly used protocols based on pH shift at highly acidic and alkaline values.

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