Our Mission

At Co-Venom, our mission is to provide high-quality venom of Leiurus quinquestriatus (DEATHSTALKER) scorpions for medical research, cancer researches and pharmaceutical applications. We source our scorpions from Upper Egypt, giving our products a fascinating and authentic origin. Our unique process ensures the high quality of the venom, making our products unique and valuable for various applications. We are dedicated to providing our customers with the best possible product for their research needs.

KNOWLEDGE OF VALUE

Scorpion venom may cause severe medical complications and possibly death if injected into the human body. Neurotoxins are the main components of scorpion venom that are known to be responsible for the pathological manifestations of envenoming. Besides neurotoxins, a wide range of other bioactive molecules can be found in scorpion venoms. Advances in separation, characterization, and biotechnological approaches have enabled not only the development of more effective treatments against scorpion envenoming, but have also led to the discovery of several scorpion venom peptides with interesting therapeutic properties. Thus, scorpion venom may not only be a medical threat to human health, but could prove to be a valuable source of bioactive molecules that may serve as leads for the development of new therapies against current and emerging diseases. The composition of scorpion venom is highly complex and heterogeneous. Up until now, small scorpion venom peptides are the most studied compounds, mainly due to their diversity and broad pharmacological properties. Accordingly to their structure, these small peptides are classified into three large superfamilies: peptides containing cysteine-stabilized (CS) α/β motifs, calcins, and non-disulfide bridged peptides (NDBPs). However, enzymes (larger proteins), mixtures of inorganic salts, free amino acids, nucleotides, amines, and lipids are also found in scorpion venom. -Peptides Containing CS α/β Motifs These peptides consist of an α-helix joined to a double or triple-stranded β-sheet via a disulfide bridge (Figure 1) [12]. These molecules present two completely conserved disulfide bonds in the Ci–Cj and Ci+4–Cj+2 positions; although some of them also exhibit an extra link connecting the two endings of the peptide chain. All scorpion peptides containing CS α/β motifs act in a similar way. Their interaction with ion channels result in blocking or modulation of the normal mode of action of these channels. Members of this superfamily can be subdivided into long or short scorpion toxin families, corresponding to their respective structures. .

Long Scorpion Toxins Peptides

Long Scorpion Toxins Peptides from the long scorpion toxin superfamily are 55–76 residue- long molecules with generally four disulfide bridges. Due to their mode of action, they can also be called sodium channel toxins (NaTxs) , as their main targets are sodium ion channels . This family can be further divided into two groups, α and β-NaTxs, depending on their specific interaction with the voltage-gated Na+ channels.

Short Scorpion Toxins

The short scorpion toxin family is composed of peptides of 23–64 residues in length with three or four disulfide bridges. These peptides, also known as potassium channel toxins (KTxs), mainly act as potassium ion channel blockers. Considering their sequences and cysteine pairs, KTxs can be divided into α, β, γ, κ, δ, λ, and ε-KTx groups. The α-KTx group, which is considered to be the largest subgroup of the short scorpion toxin family, contains 23–42 residue-long peptides with three or four disulfide bridges. The β-KTx group comprises longer chain peptides of 50–57 residues in length, Although the δ, λ, and ε-KTx groups do not contain a CS α/β motif, they are mentioned in the continuation of other KTxs. The δ-KTx group contains a Kunitz-type structural fold with a double-stranded antiparallel β-sheet flanked by an α-helix in both the C-terminal and N-terminal segments. Since the Kunitz-type structural folds are the active domains of proteins that inhibit the function of serine proteases, δ-KTxs exert both protease and potassium channel-inhibiting properties

Calcins

This small, but growing, family of scorpion toxins consists of calcium channel-modulating peptides, such as imperacalcin (imperatoxin), maurocalcin, hemicalcin, hadrucalcin, opicalcin, urocalcin, and vejocalcin. Sharing high sequence similarity (>78% identity), calcins include an ICK motif stabilized by three disulfide bridges. Calcins mainly act as agonists of ryanodine receptors (RyRs), which are intracellular ligand-activated calcium channels that are found in endoplasmic/sarcoplasmic reticulum membranes. RyRs play an essential role during excitation–contraction coupling in cardiac and skeletal muscles by releasing Ca2+ from intracellular reservoirs . In general, calcins induce long-lasting subconductance states on the RyR channels, which lead to an increase in the intracellular Ca2+ level and subsequently contractile paralysis. it has been reported that Wasabi Receptor Toxin (WaTx), from Urodacus manicatus venom, is capable of activating this receptor. This means that WaTx can cross the plasma membrane and bind to the same allosteric nexus that is covalently modified by other agonists

Non-Disulfide Bridged Peptides (NDBPs)

NDBPs are small, 13–56 amino acid-long peptides with a very heterogeneous composition. Compared to scorpion peptides with disulfide bridges, NDBPs do not present a conserved or predictable structure-function relationship, Most of these peptides are cationic molecules that display notable structural flexibility. In aqueous solutions, these peptides exhibit a random coil conformation. However, under membrane-mimicking environments, such as 50%–60% of aqueous trifluoroethanol, they readily adopt an amphipathic α-helical structure, This characteristic enables them to interact with a broad spectrum of biological targets; however, they do not have any known specific molecular targets. Enzymes ew enzymes have been found in scorpion venoms, in part because up until recently, interest has been focused on small proteins and peptides. However, during the past years, hyaluronidases, phospholipases, and metalloproteases, among other enzymes, have been detected in venoms of different scorpion species.

Other Venom Compounds

Other Venom Compounds: It has been shown that the venoms of some scorpions, including M. tamulus, contain serotonin, which is a monoamine that may cause vomiting and considerable local pain in scorpion envenomings, In their study, they found copper, zinc, calcium, magnesium, iron, lead, manganese, arsenic, and nickel ions in the venom of A. bicolor, A. crassicauda, and Leiurus quinquestriatus. They suggested that these components are associated with enzyme activity, as they probably act as enzyme cofactors