Covalent structure and some pharmacological features of native and cleaved α-KTx12−1, a four disulfide-bridged toxin from Tityus serrulatus venom
✍ Scribed by Dr A. M. C. Pimenta; P. Mansuelle; C. R. Diniz; M. F. Martin-Eauclaire
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 140 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.440
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✦ Synopsis
Abstract
A toxin with four disulfide bridges from Tityus serrulatus venom was able to compete with ^125^I‐kaliotoxin on rat brain synaptosomal preparations, with an IC~50~ of 46 nM. The obtained amino acid sequence and molecular mass are identical to the previously described butantoxin. Enzymatic cleavages in the native peptide followed by mass spectrometry peptide mapping analysis were used to determine the disulfide bridge pattern of α‐KTx~12−1~. Also, after the cleavage of the first six N‐terminal residues, including the unusual disulfide bridge which forms an N‐terminus ring, the potency of the cleaved peptide was found to decrease about 100 fold compared with the native protein. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.