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- Zafaralla, G.C. et al. (1988) Biochemistry 27, 7102.
- Alomone Labs α-Conotoxin SI inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.A. Representative time course of α-Conotoxin SI (#STC-825) inhibition of α1/β1/γ/δ nAChR currents, elicited every 50 sec by transient application of 20 µM acetylcholine, while membrane potential was held at -80 mV, and reversibly inhibited by 0.2 µM and 1 µM α-Conotoxin SI (top horizontal bars). B. Superimposed traces of α1/β1/γ/δ nAChR currents upon application of control, 0.2 µM and 1 µM α-Conotoxin SI (taken from the recording in A).
- Benie, A.J. et al. (2000) FEBS Lett. 476, 287.
- Lustig, L.R. (2006) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 288, 424.
α-Conotoxin SI is a 13-amino acid residue peptide toxin originally isolated from Conus striatus venom. The toxin’s structure is stabilized by six hydrogen bonds and disulfides between cysteine residues 2 and 7 and 3 and 131. It is a potent and selective antagonist of α1/β1/δ/γ nicotinic acetylcholine receptors (nAChRs).
Nicotinic acetylcholine receptors are ionotropic multi-subunit, neurotransmitter-gated receptors of the cholinergic system. They are responsible for mediating the effects of the neurotransmitter acetylcholine (ACh). nAChRs are assembled from one or more α subunits (α1-α10) alone or together with one or more β subunits (β1–β4)2.
α-Conotoxin SI (#STC-825) is a highly pure, synthetic, and biologically active peptide toxin.
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