α-conotoxin GID

α-conotoxin GID is a peptide originally isolated from the venom of the Conus geographus. It is composed of 19 amino acids and is folded by two disulphide bonds connecting Cys¹-Cys³ and Cys²-Cys⁴. Based on the number of amino acids between the second and the third cysteine residues (loop I) and the third and fourth cysteine residues (loop II), α-conotoxin GID belongs to the α4/7-conotoxin family. α-conotoxin GID blocks selectively neuronal nicotinic acetylcholine receptors with IC₅₀ values of 3 nM (α3β2 nicotinic receptors), 5 nM (α7) and 150 nM (α4β2). α-conotoxin GID is at least 1000-fold less potent onto the α1β1γδ, α3β4, and α4β4 nicotinic receptors. α-conotoxin GIDis a unique α4/7-conotoxin because of its ability to block both α7 and α3β2 isoforms, contrary to conotoxin PnIA or PnIB that are more selective.

α-conotoxin GID technical information

AA sequence: Ile-Arg-Asp-Gla-Cys⁵-Cys⁶-Ser-Asn-Pro-Ala-Cys¹¹-Arg-Val-Asn-Asn-Hyp-His-Val-Cys¹⁹-OH
Disulfide bonds: Cys⁵-Cys¹¹ and Cys⁶-Cys¹⁹
Length (aa): 19
Formula: C₈₄H₁₃₅N₃₁O₃₀S₄
Molecular Weight: 2185.45 Da
Modifications: Gla⁴ amino acid (gamma-carboxyglutamic acid) and Hyp¹⁶ amino acid (Hydroxyproline)
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number:
Source: Synthetic
Purity rate: > 98 %