ArticleProceedings of the National Academy of Sciences of the United States of America2024
In situ formed depot of elastin-like polypeptide-hirudin fusion protein for long-acting antithrombotic therapy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Hirudin as a Therapeutic and Brain-Delivery Platform: From Stroke to Central Nervous System Disorders.International journal of molecular sciences · 2026Review
- An engineered hirudin-albumin prodrug enables thrombus-targeted long-acting anticoagulation with reduced bleeding risk.iScience · 2026Article
- Recent advances in progress of natural anticoagulant active substances.Journal of natural medicines · 2026Review
- Self-Assembled Nanoparticles with Kynureninase-Fc Fusion Protein and Pheophorbide A for Photodynamic Immunometabolic Cancer Therapy.Journal of functional biomaterials · 2026Article
- Construction of safer hirudin-derived peptides with enhanced anticoagulant properties based on C-terminal active residue adaptation and modification.Journal of advanced research · 2026Article
- The Advances in Novel Delivery Strategies for Hirudin Against Cardiovascular Diseases.Pharmaceuticals (Basel, Switzerland) · 2026Review
- A Biomimetic Macrophage-Membrane-Fused Liposomal System Loaded with GVs-HV Recombinant Plasmid for Targeted Anti-Atherosclerosis Therapy.Pharmaceutics · 2025Article
- Recent progress on formulations of hirudin.Pharmaceutical science advances · 2025Review
- Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde.Biomolecules · 2025Article
- A designer minimalistic model parallels the phase-separation-mediated assembly and biophysical cues of extracellular matrix.Nature chemistry · 2025Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Thrombosis, induced by abnormal coagulation or fibrinolytic systems, is the most common pathology associated with many life-threatening cardio-cerebrovascular diseases. However, first-line anticoagulant drugs suffer from rapid drug elimination and risk of hemorrhagic complications. Here, we developed an in situ formed depot of elastin-like polypeptide (ELP)-hirudin fusion protein with a prodrug-like feature for long-term antithrombotic therapy. Highly secretory expression of the fusion protein was achieved with the assistance of the Ffu312 tag. Integration of hirudin, ELP, and responsive moiety can customize fusion proteins with properties of adjustable in vivo retention and controllable recovery of drug bioactivity. After subcutaneous injection, the fusion protein can form a reservoir through temperature-induced coacervation of ELP and slowly diffuse into the blood circulation. The biological activity of hirudin is shielded due to the N-terminal modification, while the activated key proteases upon thrombus occurrence trigger the cleavage of fusion protein together with the release of hirudin, which has antithrombotic activity to counteract thrombosis. We substantiated that the optimized fusion protein produced long-term antithrombotic effects without the risk of bleeding in multiple animal thrombosis models.
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Registered trials
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.