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Updated: May 2, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
Functional and structural study comparing the C-terminal amidated β-neurotoxin Ts1 with its isoform Ts1-G isolated
V A Coelho1, C M Cremonez1, F A P Anjolette1
1Department of Physics and Chemistry, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Av. do Café, s/n, 14040-903 Ribeirão Preto, SP, Brazil.
Abstract:
Mature Ts1, the main neurotoxin from Tityus serrulatus venom, has its C-terminal Cys amidated, while the isolated isoform of Ts1, named Ts1-G, keeps the non-amidated Gly residue at the C-terminal region, allowing the study of the comparative functional importance of amidation at the C-terminal between these two native toxins. Voltage dependent sodium current measurements showed that the affinity of Ts1-G for sodium channels is smaller than that of the mature Ts1, confirming the important role played by the C-terminal amidation in determining Ts1 activity.
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