ArticleMolecules (Basel, Switzerland)2025
Activity of Potassium Channel BmK-NSPK Inhibitor Regulated by Basic Amino Acid Residues: Novel Insight into the Diverse Peptide Pharmacology.
Article in Molecules (Basel, Switzerland), 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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1 citing paper in PubMed.
- From venom peptides to neurotherapeutics: BmK defensins and short-chain peptides as modulators of ion channels.Frontiers in pharmacology · 2026Review
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6 authors.
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Abstract
The molecular interactions between venomous peptides and potassium channels have extensively enriched the knowledge of diverse peptide pharmacology, and the in-depth understanding of general features of the various peptide functions remains a formidable challenge. In this work, the role of peptide basic residues in peptide pharmacology was first investigated. Although the venomous BmK-NSPK peptide had the critically conserved functional residues occurring in its similar and potent potassium channel-inhibiting peptides, it was a remarkably weak inhibitor of potassium channels due to fewer basic residues. Additionally, 1 μM BmK-NSPK only inhibited 1.2 ± 1.0%, 1.7 ± 0.70%, 2.3 ± 0.49% and 5.4 ± 0.70% of hKv1.1, hKv1.2, hKv1.3 and hKv1.6 channel currents. The introduction of one or two basic residues in BmK-NSPK-I15K, BmK-NSPK-I18K, BmK-NSPK-I26K and BmK-NSPK-I18K/I26K could not improve BmK-NSPK activity. The modifications of more than three basic residues were found to continuously improve BmK-NSPK activity, and the corresponding BmK-NSPK-7K and BmK-NSPK-8K mutants could effectively inhibit hKv1.3 channel with IC
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