Functional and structural study comparing the C-terminal amidated beta-neurotoxin Ts1 with its isoform Ts1-G isolated from Tityus serrulatus venom

Author(s)

Coelho, V. A. ^[1] ; Cremonez, C. M. ^[1] ; Anjolette, F. A. P. ^[1] ; Aguiar, J. F. ^[2] ; Varanda, W. A. ^[2] ; Arantes, E. C. ^[1]

Affiliation

^[1] Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Chem & Phys, BR-14040903 Ribeirao Preto, SP - Brazil

^[2] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Physiol, BR-14049900 Ribeirao Preto, SP - Brazil

• Document type: Journal article
• Source: Toxicon; v. 83, p. 15-21, JUN 1 2014.
• Web of Science Citations: 11

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-arnidated 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. (C) 2014 Elsevier Ltd. All rights reserved. (AU)

• FAPESP's process: 10/16600-9 - Calcium handling and secretion in Leydig cells
• Grantee: Wamberto Antonio Varanda
• Support Opportunities: Regular Research Grants
• FAPESP's process: 08/07373-9 - Structural and functional characterization of the precursor Ts1, the major toxin from Tityus serrulatus venom
• Grantee: Vinicius Adriano Coelho
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• FAPESP's process: 08/10761-0 - Isolation, structural and functional characterization of a new alpha-neurotoxin from Tityus serrulatus scorpion venom
• Grantee: Eliane Candiani Arantes Braga
• Support Opportunities: Regular Research Grants