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

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 betwe...

Full description

Saved in:

Bibliographic Details
Published in:	Toxicon (Oxford) Vol. 83; pp. 15 - 21
Main Authors:	Coelho, V.A., Cremonez, C.M., Anjolette, F.A.P., Aguiar, J.F., Varanda, W.A., Arantes, E.C.
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01-06-2014
Subjects:	Amino Acid Sequence Animals Arthropod Proteins - chemistry Arthropod Proteins - isolation & purification Arthropod Proteins - toxicity Blood Glucose - drug effects C-terminal amidation Chemical Fractionation Insect Proteins - chemistry Insect Proteins - isolation & purification Insect Proteins - toxicity Male Mice, Inbred Strains Molecular Sequence Data Neurotoxins - chemistry Neurotoxins - isolation & purification Neurotoxins - toxicity Protein Isoforms - chemistry Protein Isoforms - isolation & purification Protein Isoforms - toxicity Scorpion Venoms - chemistry Scorpion Venoms - isolation & purification Scorpion Venoms - toxicity Scorpions Sequence Alignment Tityus serrulatus venom Ts1 isoform Voltage gated sodium channels β-Neurotoxin Ts1 isoform Nav channel Tityus serrulatus venom β-Neurotoxin Voltage gated sodium channels C-terminal amidation NaScTx
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	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. •Ts1-G from Tityus serrulatus scorpion venom was isolated and characterized.•Ts1-G keeps the non-amidated Gly residue at the C-terminal region.•The affinity of Ts1-G for voltage-sodium channels is smaller than that of Ts1.•C-terminal amidation is important for Ts1 activity.
ISSN:	0041-0101 1879-3150
DOI:	10.1016/j.toxicon.2014.02.010