ArticleInternational journal of nanomedicine2025
Delivery of Polypeptide Drugs Using Nanoparticles Made of Recombinant Spider Silks Derived From MaSp4 Protein.
Article in International journal of nanomedicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed.
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Spider silk protein is a biocompatible and biodegradable protein that can self-assemble into various morphological materials for biomedical applications including drug delivery carriers. Spiders can spin up to seven types of silk fibers, each containing multiple silk proteins. Despite the numerous potential applications of these silk proteins, comprehensive and in-depth research on their specific roles and efficacy in drug delivery has yet to be conducted. The authors designed three new bioengineered spider silk proteins (M4R2, M4R4, and M4R6) and examined its property as a carrier of polypeptided drugs. Materials and Methods: To obtain the M4R2, M4R4, and M4R6 proteins, three constructs comprising 2, 4, and 6 repeat units of Araneus ventricosus major ampullate spidroin 4 (MaSp4) were engineered for prokaryotic expression using the Results: The three bioengineered silk proteins, M4R2, M4R4, and M4R6, were constructed, produced, and purified. These proteins exhibit self-assembly properties and formed particles. Furthermore, the these particles were not cytotoxic and had similar particle sizes but differed in loading efficiency and drug release rate. The loading of drugs into the M4R2 particles was more efficient (>95%) than that into the M4R4 and M4R6 particles. In addition, the continuous release of ChMAP-28 from M4R2 particles over 30 days indicates its potential as a sustained-release carrier for positively charged peptide drugs. The high stability, excellent loading efficiency, and sustained-release performance of M4R2 particles make them an ideal choice for the delivery of positively charged peptide drugs. Conclusion: We developed three recombinant silk proteins, M4R2, M4R4, and M4R6, demonstrating that M4R2 particles, with stable colloidal properties, high loading efficiency of positively charged drugs, and controlled release rates, are promising new particulate drug carrier systems for the delivery of polypeptided drugs.
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Registered trials
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