Conus vexillum Alpha-conotoxin VxXXC

Cloning, expression and functional characterization of the superfamily D conotoxin Lt28.1 with a previously undescribed cysteine ​​pattern.

As a class of peptides containing 10 cysteine ​​residues (-C-CC-C-CC-C-C-C-C-), D-superfamoxins (D-conotoxins) can act specifically on nicotinic acetylcholine receptors (nAChRs). Consistent with the conserved signal peptides of D-conotoxins, seven D-conotoxin precursor sequences in a previously undescribed Cys order (-C-C-C-CC-C-C-C-C-) were identified by PCR-RACE methodology in the present study. Sequence alignment revealed that the signal peptide regions were identical to Conus vexillum D-VxXXA, and the mature peptides were almost different from the D-conotoxins. Phylogenetic tree analyzes showed that they had low homology to reported virulent toxins with 10 cysteine ​​residues (<35%) and were on a separate branch of the phylogenetic tree. In addition, a previously undescribed toxin D from the Lt28.1 superfamily was expressed in Pichia pastoris and then functionally characterized. Results showed that recombinant Lt28.1 targeted α9α10 nAChRs but not other nAChR subtypes. These results identified a new branch of the D superfamily and furthered our understanding of the targets and potential application of D-conotoxins.

The role of defensive environmental interactions in the evolution of toxins.

Venoms consist of complex mixtures of peptides that have evolved for predation and defense purposes. Surprisingly, some carnivorous cone snails can inject different toxins in response to predatory or defensive stimuli, providing a unique opportunity for the separate study of how different environmental stresses contribute to toxin diversity. Here, we report the unusual defensive strategy of the Rhizoconus subgenus of cone snails. The defensive venom of this worm-hunting subspecies is unusually simple, consisting almost exclusively of αD cone toxins rather than the ubiquitous defensive toxins found in the more complex defensive venom of fish- and slug-hunting cone snails. A divided poison gland similar to that seen in other food groups facilitates the spread of this defensive poison. Transcriptional analysis of the venom gland of Conus vexillum revealed that αD cone toxins are the major transcripts, with known numbers less than 15, and four new types of virulent toxins also discovered with potential roles in prey capture. Our phylogenetic and molecular analysis of the virulent αD toxin from five cone snail subgenerations indicates that it causally evolved as part of a defense strategy in the subgenus Rhizoconus. Thus, our results demonstrate an important defense role in toxin development.

Evolution of αD-Conopeptides that target neuronal nicotinic acetylcholine receptors.

Cone sea snail (Conus spp.) venoms consist of many proteins and peptides that exhibit a variety of biological activities, such as ion channels and receptors. Peptides that act on neuronal nicotinic acetylcholine receptors belong to several peptide superfamilies, including the recently described αD conopeptides, which are peptide homologues identical at 47 to 49 amino acids. Among the venom glands of 27 Conus species analyzed by cDNA cloning, αD conopeptide precursors were identified in only four species: C. betulinus, C. capitaneus, C. mustelinus, and C. vexillum. Phylogenetic analysis of the relationships between the αD conopeptides revealed that they belong to clades, which are characterized by the AVV and EMM motifs in the signal peptide sequence.

A new inhibitor of the α9α10 nicotinic acetylcholine receptor from Conus vexillum identifies a new toxic family of malignant toxins.

CTx selectively targets a variety of ion channels and receptors, making them widely used tools for examining nervous system function. Conotoxins have previously been classified into superfamilies based on signal sequences and families based on cysteine ​​framework and biological target. Here we describe the cloning and characterization of a new conotoxin, from Conus vexillum, named αB-conotoxin VxXXIVA. The peptide does not belong to any of the supertoxin families described above, and the arrangement of Cys residues is unique among conopeptides. Furthermore, unlike previously characterized conopeptide toxins, which are initially expressed as peptide precursors with a signal sequence, a ‘pro’ region, and a d.

Conus vexillum Alpha-conotoxin VxXXC

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Recombinant Conus vexillum Alpha-conotoxin VxXXC

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Recombinant Conus vexillum Alpha-conotoxin VxXXC

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Recombinant Conus vexillum Alpha-conotoxin VxXXC

RPC28238-100ug Biomatik Corporation 100ug 765.5 EUR

Recombinant Conus vexillum Alpha-conotoxin VxXXC

RPC28238-1mg Biomatik Corporation 1mg 2959.2 EUR

Recombinant Conus vexillum Alpha-conotoxin VxXXC

RPC28238-20ug Biomatik Corporation 20ug 448.1 EUR

Conotoxin SI - Alpha (Conus striatus)

063-04 PHOENIX PEPTIDE 100 μg 92.88 EUR

Conotoxin MI (Conus magus)

063-03 PHOENIX PEPTIDE 100 μg 81 EUR

Conotoxin GI (Conus geographus)

063-02 PHOENIX PEPTIDE 100 μg 81 EUR

Conotoxin GS (Conus geographus)

063-14 PHOENIX PEPTIDE 100 μg 316.44 EUR

Conotoxin MVIIC - Omega (Conus magus)

063-15 PHOENIX PEPTIDE 100 μg 189 EUR

Conotoxin GIIIB - Mu (Conus geographus)

063-05 PHOENIX PEPTIDE 100 μg 214.92 EUR

Conotoxin SVIB - Omega (Conus striatus)

063-16 PHOENIX PEPTIDE 100 μg 230.04 EUR


Conus vexillum toxin causes oxidative stress in Ehrlich ascites carcinoma cells: insights into the mechanism of induction.

Venoms from cone snails (genus Cone) are estimated to contain more than 100,000 different small peptides with a wide range of pharmacological and biological actions. Some of these peptides have become potential therapeutic agents and molecular tools to understand the biological functions of the nervous and cardiovascular systems. In this study, we examined the cytotoxic and anticancer properties of the worm-eating cone sea snail Conus vexillum (collected in Hurghada, Sharm El Sheikh and the Red Sea, Egypt) and suggested possible mechanisms. The in vitro cytotoxic effects of Conus toxin were evaluated against Ehrlich ascites carcinoma (EAC) cells.

Conic toxin treatment resulted in concentration-dependent cytotoxicity, as demonstrated by the lactate dehydrogenase leak assay. The effects of apoptosis were measured in vivo by measuring the levels of reactive oxygen species and oxidative defense factors in albino mice injected with EAC cells. Conus toxin (1.25 mg/kg) caused a significant (P < 0.05) increase in several biomarkers of oxidative stress (lipid peroxidation, CRP content, and intermediate reactive nitrogen) in EAC at 3, 6, 9, and 12 h. after injection of the poison. Conus toxin significantly (P < 0.05) reduced the activities of oxidative defense enzymes (catalase and superoxide), as well as the general antioxidant capacity of EAC cells, as indicated by decreased glutathione levels.

These results demonstrate the cytotoxic capacity of the C. vexillum toxin by stimulating oxidative stress mechanisms in cancer cells and suggest that the toxin contains novel molecules with potential anticancer activity.

Nonspecific variation in the venom of the worm-eating cone snail Conus vexillum.

A combination of proteomic and biochemical assays was used to examine differences in Conus vexillum venom taken from two sites (Hurghada and Sharm El Sheikh) in the Red Sea, Egypt. Using MALDI/TOF-MS, an appreciable degree of intraspecific variability was determined between venom samples from both locations. To assess variability in the cytotoxic effects of Conus toxin, mice were injected with the same dose at each site. Oxidative stress biomarkers [malondialdehyde (MDA), protein carbonyl content (PCC)], antioxidants [glutathione (GSH), superoxide dismutase (SOD), catalase (CAT)], total antioxidant capacity (TAC), and nitric oxide (NO) , were measured 3, 6, 9 and 12 h after venom injection. The toxins caused a significant increase in the levels of PCC, MDA, NO, GSH and CAT. The toxins significantly inhibit SOD activity and reduce TAC. Toxicological data showed that the poison obtained from Hurghada was stronger than that obtained from Sharm El-Sheikh. It can be concluded that: (1) venom of the same Conus species from different regions is highly diverse (2) toxins from different locations reflect different differences in venom potency and (3) cytotoxic effects of C. may be different . attributed to its ability to induce oxidative stress.



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