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Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
Structural highlights
FunctionKBX3_HOFGE Has antibacterial activity against B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic activities. Since cell lysis occurs at the tested concentrations, observation of activity on potassium channels is impossible.[1] Blocks Kv1.1/KCNA1 (IC(50)=185 nM) potassium channels. Shows a weak hemolytic activity.[2] [3] Publication Abstract from PubMedScorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channel-blocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold. Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi.,Flores-Solis D, Toledano Y, Rodriguez-Lima O, Cano-Sanchez P, Ramirez-Cordero BE, Landa A, Rodriguez de la Vega RC, Del Rio-Portilla F FEBS Lett. 2016 Jun 17. doi: 10.1002/1873-3468.12255. PMID:27314815[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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