7m1e
Structural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domainsStructural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domains
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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