ArticlePloS one2011
SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 64 citations in OpenAlex.
- Discovery and Functional Characterization of Kunitz-Type Toxins from the Tetrodotoxin-Bearing Flatworm Planocera Multitencaculata.Marine biotechnology (New York, N.Y.) · 2026Article
- Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential.International journal of molecular sciences · 2025Review
- Properties and Pharmacology of Scorpion Toxins and Their Biotechnological Potential in Agriculture and Medicine.Toxins · 2025Review
- Functional characterization of a common XIa inhibitory Kunitz-domain Shp4 from nine schistosoma secreted proteins with diverse C-terminal fragments.PLoS neglected tropical diseases · 2025Article
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- Kunitz-Type Peptides from Sea Anemones Protect Neuronal Cells against Parkinson's Disease Inductors via Inhibition of ROS Production and ATP-Induced P2X7 Receptor Activation.International journal of molecular sciences · 2022Article
- Peptide Inhibitors of Kv1.5: An Option for the Treatment of Atrial Fibrillation.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Article
- Evolutionary Aspects of the Structural Convergence and Functional Diversification of Kunitz-Domain Inhibitors.Journal of molecular evolution · 2020Review
- A Kunitz-type peptide fromThe journal of venomous animals and toxins including tropical diseases · 2020Article
- Combined transcriptomic and proteomic analysis reveals a diversity of venom-related and toxin-like peptides expressed in the mat anemone Zoanthus natalensis (Cnidaria, Hexacorallia).Archives of toxicology · 2019Article
- Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous ScorpionToxins · 2019Article
- Article
- Proteomic Analysis of Novel Components ofToxins · 2019Article
- Scorpion toxins targeting Kv1.3 channels: insights into immunosuppression.The journal of venomous animals and toxins including tropical diseases · 2019Article
- Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the ScorpionMolecules (Basel, Switzerland) · 2018Article
- Schistosoma mansoni SmKI-1 serine protease inhibitor binds to elastase and impairs neutrophil function and inflammation.PLoS pathogens · 2018Article
- Screening, Purification and Characterization of Protease Inhibitor fromBioinformation · 2018Article
- Tentacle Transcriptome and Venom Proteome of the Pacific Sea Nettle, Chrysaora fuscescens (Cnidaria: Scyphozoa).Toxins · 2016Article
- Functional expression of a novel Kunitz type protease inhibitor from the human blood fluke Schistosoma mansoni.Parasites & vectors · 2015Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundKunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of venomous animals. However, no Kunitz-type peptides from scorpion venom have been functionally characterized. PRINCIPAL
findingsA new Kunitz-type venom peptide gene precursor, SdPI, was cloned and characterized from a venom gland cDNA library of the scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of 59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin inhibitory activity with high potency (K(i) = 1.6×10(-7) M) and thermostability.
conclusionsThe results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-type venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived from scorpion venom, and it represents a new class of Kunitz-type venom peptides.
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