α-conotoxin-GID

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Blocker of α3β2, α7 and α4β2 nAChRs

 α-conotoxin GID is a conopeptide 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 GID is 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.

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Description

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 g/mol
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: > 95 %

Design and synthesis of α-conotoxin GID analogues as selective α4β2 nicotinic acetylcholine receptor antagonists

Inhibition of Neuronal Nicotinic Acetylcholine Receptor Subtypes by α-Conotoxin GID and Analogues

Isolation, Structure, and Activity of GID, a Novel 4/7-Conotoxin with an Extended N-terminal Sequence

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    α-conotoxin-GID

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