Novel Scorpion Toxin ω-Buthitoxin-Hf1a Selectively Inhibits Calcium Influx via Ca_V3.3 and Ca_V3.2 and Alleviates Allodynia in a Mouse Model of Acute Postsurgical Pain.

ABSTRACT: Venom peptides have evolved to target a wide range of membrane proteins through diverse mechanisms of action and structures, providing promising therapeutic leads for diseases, including pain, epilepsy, and cancer, as well as unique probes of ion channel structure-function. In this work, a high-throughput FLIPR window current screening assay on T-type Ca_V3.2 guided the isolation of a novel peptide named ω-Buthitoxin-Hf1a from scorpion Hottentotta franzwerneri crude venom. At only 10 amino acid residues with one disulfide bond, it is not only the smallest venom peptide known to target T-type Ca_Vs but also the smallest structured scorpion venom peptide yet discovered. Synthetic Hf1a peptides were prepared with C-terminal amidation (Hf1a-NH₂) or a free

SUBMITTER: Wang D 

PROVIDER: S-EPMC11084959 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature