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Biochim Biophys Acta Biomembr ; 1865(1): 184057, 2023 01 01.
Article in English | MEDLINE | ID: mdl-36240866

ABSTRACT

Ts17 was purified from the venom of the scorpion Tityus serrulatus, the most dangerous scorpion species in Brazil. The activity on Nav1.1-Nav1.7 channels was electrophysiologically characterized by patch-clamp technique. Ts17 amino acid sequence indicated high similarity to alpha-scorpion toxins; however, it presented beta-toxin activity, altering the kinetics of the Na+-channels. The most affected subtypes during activation (with and without prepulse) and inactivation phases were Nav1.2 and Nav1.5, respectively. For recovery from inactivation, the most affected voltage-gated sodium channel was Nav1.5. Circular dichroism spectra showed that Ts17 presents mainly ß-sheet and unordered structures at all analyzed pHs, and the maximum value of α-helix was found at pH 4.0 (13.3 %). Based on the results, Ts17 might be used as a template to develop a new cardiac drug. Key contribution Purification of Ts17 from Tityus serrulatus, electrophysiological characterization of Ts17 on voltage-gated sodium channel subtypes, ß-toxin classification.


Subject(s)
Scorpion Venoms , Voltage-Gated Sodium Channels , Animals , Scorpions/chemistry , Scorpion Venoms/pharmacology , Scorpion Venoms/chemistry , Amino Acid Sequence , Patch-Clamp Techniques
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