화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.411, No.4, 673-678, 2011
A naturally-occurring carboxyl-terminally truncated alpha-scorpion toxin is a blocker of sodium channels
alpha-Scorpion toxins constitute a multigene family of evolutionarily conserved venom peptides that inhibit sodium channel inactivation and increase its peak current. Here, we describe the characterization of a new alpha-scorpion toxin gene expressed in the venom gland of Mesobuthus eupeus that encodes a carboxyl-terminally truncated product of 38 residues (named MeuNaTx alpha(NT)-1). Synthetic MeuNaTx alpha(NT)-1 was oxidized to form two disulfide bridges in an alkaline environment and the refolded peptide exhibits different structure and function from the classical alpha-scorpion toxin. MeuNaTx alpha(NT)-1 blocks sodium channels on rat dorsal root ganglia (DRG) neurons without impact on the inactivation of the channels. This work provides a clue for evolution-guided design of channel blockers for therapeutic aims. (C) 2011 Elsevier Inc. All rights reserved.