ArticleBMC biotechnology2018
Novel hemostatic biomolecules based on elastin-like polypeptides and the self-assembling peptide RADA-16.
Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Emerging biomimetic biopolymer-based composites: advancing accessible and sustainable neural disease models and therapeutics.Frontiers in bioengineering and biotechnology · 2025Review
- Recent advances in biopolymer-based hemostatic materials.Regenerative biomaterials · 2022Review
- Advances in the development and optimization strategies of the hemostatic biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- Application of Thermoresponsive Intrinsically Disordered Protein Polymers in Nanostructured and Microstructured Materials.Macromolecular bioscience · 2021Review
- Peptide-based topical agents and intravenous hemostat for rapid hemostasis.RSC medicinal chemistry · 2020Review
- Coupling synthetic biology and programmable materials to construct complex tissue ecosystems.MRS communications · 2019Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSafe and effective hemostatic materials are important for reducing mortality resulting from excessive hemorrhage. In this work, new biomaterials with hemostatic effects were created by fusing the gene coding for RADA-16, a self-assembling peptide with the sequence RADARADARADARADA, to the 3'-end of the open reading frame (ORF) encoding elastin-like polypeptides through gene recombination.
resultsThe fusion proteins, termed 36R, 60R and 96R, were solubly over-expressed in Escherichia coli BL21 (DE3) based on genetic manipulation of the high-efficiency prokaryotic expression vector pET28a (+) and bacterial transformation. Western Blot analysis showed that the over-expressed proteins were the target fusion proteins. The target proteins 36R with 94.72% purity, 60R with 96.91% purity and 96R with 96.37% purity were prepared using an inverse phase transition cycle at 65 °C followed by His-tag affinity chromatography. The proliferation results of the mouse fibroblast cell line L929 and hippocampus neuron cell line HT22 indicated that the fusion proteins did not cause obvious cell toxicity. The lyophilized spongy film of the purified 36R, 60R and 96R could stop the hemorrhage of a 2 × 2 mm bleeding wound in the mouse liver after 27.21 ± 1.92 s, 18.65 ± 1.97 s and 15.85 ± 1.21 s, respectively. The hemostasis time was 21.23 ± 1.84 s for rat-tail collagen and 14.44 ± 1.33 s for RADA-16 lyophilized on gauze. The hemostatic time of three treated groups were all significantly superior to that of the negative control without any hemostasis treatment, which spontaneously stopped bleeding after 37.64 ± 1.34 s. Statistical analysis showed that the spongy film with purified 96R exhibited an exciting hemostatic effect that was superior to rat-tail collagen and close to that of RADA-16 lyophilized on gauze.
conclusionsThese results revealed that the fusion proteins achieved by gene recombination technology could serve as a promising hemostatic material.
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