AA sequence: Cys1-Phe-Ile-Arg-Asn-Cys6-Pro-Lys-Gly-NH2
(Disulfide bond between Cys1-Cys6)
Length (aa): 9
Formula: C44H70N15O10S2
Molecular Weight: 1033.26 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number:
Source: Synthetic
Purity rate: > 97 %
Lys-conopressin-G
Vasopressin-like peptide
Lys-conopressin G is a conopeptide that was isolated from conus imperialis. This vasopressin-like peptide induces scratching and grooming behavior when injected into mice.
Contact us
Change currency
Isolation of Lys-conopressin-G from the venom of the worm-hunting snail, Conus imperialis
Vasopressin homologs have previously been isolated from the venom of fish-hunting cone snails. We investigated whether a vasopressin-like peptide is found in the worm-hunter, Conus imperialis. Using i.c. injections in mice, we isolated a peptide from the venom of C. imperialis which induces scratching and grooming behavior characteristic of the conopressins. Biochemical characterization showed that this peptide is identical to Lys-conopressin-G. The results led us to speculate that the vasopressin-like peptides in Conus venoms may be examples of an evolving conversion of endogenous peptides for specialized venom uses.
Nielsen DB, et al. (1994) Isolation of Lys-conopressin-G from the venom of the worm-hunting snail, Conus imperialis. Toxicon. PMID: 7940591
Characterization of peptides from conus geographus and conus striatus venoms.
The vasopressin-oxytocin family of peptides is of very ancient lineage, found in organisms as diverse as hydra and man. Although these peptides have been intensively studied in vertebrates, the presumably more extensive invertebrate series was defined primarily by immunological methods. In this report, we describe the purification and structures of two peptides of the vasopressin-oxytocin family from molluscs (“Conopressins”), which were found in the venom of fish-hunting marine snails of the genus Conus. The biological activity observed when the two snail peptides are injected intracerebrally into mice is very similar to that elicited by the vertebrate neurohypophyseal hormones and presumably reflects their actions upon a common receptor in the brain. The sequences of the purified peptides reveal unique features not found in the vertebrate peptide series, most notably an additional positive charge. These are the first members of the invertebrate series of the vasopressin-oxytocin family to be characterized biochemically. The sequences of these peptides are: from Conus geographus venom, Lys-conopressin-G, Cys-Phe-Ile-Arg-Asn-Cys-Pro-Lys-Gly-NH2; and from Conus striatus venom, Arg-conopressin-S, Cys-Ile-Ile-Arg-Asn-Cys-Pro-Arg-Gly-NH2.
Lourdes J. et al. (1987) Characterization of peptides from conus geographus and conus striatus venoms. J Biol Chem. PMID: 3680228