ArticleToxins2016
The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels.
Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
- Diversity and Bioprospection of Functional Proteins from Sea AnemoneMarine drugs · 2026Article
- Marine Antimicrobial Peptides: Advances in Discovery, Multifunctional Mechanisms, and Therapeutic Translation Challenges.Marine drugs · 2025Review
- Article
- Insights into Octopus maya cathepsins from metatranscriptome and genome: structure evolutionary relationships and functional role prediction in digestive processes.Biology open · 2025Article
- The proteotranscriptomic characterization of venom in the white seafanOpen biology · 2025Article
- Sea Anemone Kunitz Peptide HCIQ2c1 Reduces Histamine-, Lipopolysaccharide-, and Carrageenan-Induced Inflammation via the Suppression of Pro-Inflammatory Mediators.International journal of molecular sciences · 2025Article
- Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025Article
- Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo.Marine drugs · 2024Article
- Voltage-Gated KMarine drugs · 2024Review
- Diversity analysis of sea anemone peptide toxins in different tissues of Heteractis crispa based on transcriptomics.Scientific reports · 2024Article
- Venomics Reveals the Venom Complexity of Sea AnemoneMarine drugs · 2024Article
- Spatial Distribution and Biochemical Characterization of Serine Peptidase Inhibitors in the Venom of the Brazilian Sea AnemoneMarine drugs · 2023Article
- The Potassium Channel Blocker β-Bungarotoxin from the KraitBiomedicines · 2023Article
- Recombinant Analogs of Sea Anemone Kunitz-Type Peptides Influence P2X7 Receptor Activity in Neuro-2a Cells.Marine drugs · 2023Article
- Article
- Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae).Biomolecules · 2022Article
- 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
- AsKC11, a Kunitz Peptide fromMarine drugs · 2022Article
- Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds.Marine drugs · 2021Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bovine pancreatic trypsin inhibitor (BPTI)-Kunitz-type protein ShPI-1 (UniProt: P31713) is the major protease inhibitor from the sea anemone Stichodactyla helianthus. This molecule is used in biotechnology and has biomedical potential related to its anti-parasitic effect. A pseudo wild-type variant, rShPI-1A, with additional residues at the N- and C-terminal, has a similar three-dimensional structure and comparable trypsin inhibition strength. Further insights into the structure-function relationship of rShPI-1A are required in order to obtain a better understanding of the mechanism of action of this sea anemone peptide. Using enzyme kinetics, we now investigated its activity against other serine proteases. Considering previous reports of bifunctional Kunitz-type proteins from anemones, we also studied the effect of rShPI-1A on voltage-gated potassium (Kv) channels. rShPI-1A binds Kv1.1, Kv1.2, and Kv1.6 channels with IC50 values in the nM range. Hence, ShPI-1 is the first member of the sea anemone type 2 potassium channel toxins family with tight-binding potency against several proteases and different Kv1 channels. In depth sequence analysis and structural comparison of ShPI-1 with similar protease inhibitors and Kv channel toxins showed apparent non-sequence conservation for known key residues. However, we detected two subtle patterns of coordinated amino acid substitutions flanking the conserved cysteine residues at the N- and C-terminal ends.
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