ArticleBioresources and bioprocessing2025
Heterologous expression and functional characterization of recombinant arenin to assess its anticancer and wound-healing potential.
Article in Bioresources and bioprocessing, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Insulin Resistance, Anti-inflammatory, and AntioxidantBiotechnology reports (Amsterdam, Netherlands) · 2026Article
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7 authors.
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Abstract
Arenin is a cystine-rich Kunitz-type protease inhibitor originally isolated from the skin secretion of the tree frog Dryophytes arenicolor, whose limited natural yield has hindered comprehensive functional studies. In this work, we established an efficient recombinant production system in Escherichia coli and evaluated its anticancer and wound-healing properties. A codon-optimized arenin gene, fused to an N-terminal 6 × His-TEV tag, was cloned into a T7-lac expression cassette. IPTG induction at 30 °C and 37 °C revealed distinct temperature-dependent partitioning: at 30 °C, arenin predominantly accumulated in the soluble fraction, whereas at 37 °C, it was confined to inclusion bodies. Both strategies yielded ≥ 90% pure peptide, producing 7.8 ± 0.6 mg and 12.4 ± 1.0 mg per 250 mL culture, respectively. Bioassays showed that HDFa fibroblasts tolerated 31.25-500 µg mL
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