Structural highlights
FunctionPublication Abstract from PubMedScorpine is an antimicrobial and antimalarial peptide isolated from Pandinus imperator scorpion venom. As there are few functional and structural studies reported on scorpine-like peptides, we investigated the recombinant truncated N- and C-terminal domains as well as complete scorpine using biological assays and determined the N- and C-terminal structures using solution nuclear magnetic resonance. The study was conducted using recombinant N- and C-terminal peptides and complete scorpine expressed in Escherichia coli. The results showed that N-scorpine presented a random coil structure in water and adopted alpha-helical folding in the presence of 50% trifluoroethanol (TFE). C-scorpine contains three disulfide bonds with two structural domains: an unstructured N-terminal domain in water that can form a typical secondary alpha-helix structure in 50% TFE and a C-terminal domain with the CS-alphabeta motif. Our findings demonstrate cytolytic activity associated with C-scorpine, N-scorpine, and scorpine, as well as channel blocking activity associated with the C-scorpine domain. Structural and functional studies of scorpine: A channel blocker and cytolytic peptide.,Lopez-Giraldo E, Carrillo E, Titaux-Delgado G, Cano-Sanchez P, Colorado A, Possani LD, Rio-Portilla FD Toxicon. 2022 Nov 24;222:106985. doi: 10.1016/j.toxicon.2022.106985. PMID:36436588[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 10:07, 21 December 2022.