Entering into force on 12 October 2014, The Nagoya Protocol on Access and Benefit-sharing is an international agreement that aims at sharing the benefits arising from the use of genetic resources in a fair and equitable way. As our library comprises animals that were either acquired prior to 12 October 2014 or sourced from countries that have not implemented the required legislation, it is exempt from this agreement. Our venoms are certified to this effect.
Just like in drug discovery, good active ingredients in cosmetics act on relevant targets. Venoms can be made safe for cosmetic use by only selecting the key active peptide and not using the parts involved in the toxic pathways. This is the essence of our VenomSELECT™ service.
Visit the Mibelle Biochemistry website to read about one of our early success stories – SensAmone-P5.
See our cosmetics page for further information.
1-10 kDa peptides predominate in numerous venoms. Larger peptides, proteins, and small molecules (such as acylpolyamines) are also present. The exact distribution is dependent on the species.
Whole venoms are soluble up to approximately 300 mg/ml in aqueous buffers. Individual fractions may vary, depending on their hydrophobicity.
Yes. There are venom peptides already on the market, for example Byetta®, Echistatin and Prialt®. Venoms have also been used in the discovery of other drugs, such as angiotensin converting enzyme (ACE) inhibitors like Captopril®, and peptomimetics like Eptifibatide.
Venom peptides used in drug discovery, cosmetics and crop science are poorly recognised by the immune systems of animals. They rarely illicit an immune response, even when one is needed. Many venom components, especially small peptides, are poorly immunogenic. Whole snake venoms do elicit immune reactions, including anaphylaxis, in humans. Due to of the risk of whole venom sensitisation, we operate strict, safe systems of work, including local exhaust ventilation to protect our staff.
Animal venoms have not evolved to cure our diseases. The targets that venoms have evolved to hit in their prey have also evolved in humans and are highly conserved. As an example, a Na+ ion channel vital for insect life has also evolved in humans but is involved in pain transmission. A venom that evolved to kill insects can therefore have potential as a therapeutic agent in treating pain in humans. Many venoms have actions on their prey that are desirable for treating specific diseases, e.g. snake venoms that lower blood pressure will have potential in treating hypertension, while some spider venoms block pain receptors. See our drug discovery page for more information.
Arthropod venoms, for example, have evolved to kill insects effectively and many are selective to particular species. Some snakes also prey on invertebrates and have invertebrate-specific toxins. Better yet, these compounds are biodegradable and non-pollutant to the environment.
Venoms contain several hundred components, which is why we provide them in a 2D fractionated T-VDA™. A typical T-VDA™ may contain 1-5 entities per well and avoids the complex poly-pharmacology of the whole venom while being less expensive than a single entity array.
Our venom fractions are no more dangerous to work with than many other pharmaceutical actives. Venoms do contain some toxic compounds (proteins and peptides), but this potency is what makes them useful for research; we supply full Safety Data Sheets with our shipments and will happily send them in advance. Safety systems used for screening pharmaceutical actives – such as local exhaust ventilation for dissolving powders and autoclaves for disposing of any surplus – are suitable for use when preparing venoms and venom fractions for screening.
For T-VDA™ solutions, the 200 ng/well of protein supplied is enough for up to 50 µl final assay volume for single dose screening. The Diversity Set is useful for larger reaction volumes of up to 1 ml.
This depends on your assay sensitivity, but typically venom peptides are active in the picomolar – nanomolar range.
We advise you to avoid the use of DMSO, because it can sulphonate proteins and peptides. There is the potential to modify the unknown, thus making deconvolution and identification difficult.
Our lyophilised T-VDA™ plates are shipped at ambient temperature and are stable under these conditions for several weeks. We recommend storage at -20 °C upon receipt.
Venoms are intrinsically very stable proteins and remain stable and active in most biological (biochemical and cell-based) assays.
200 ng/well of protein is supplied in our standard arrays. The amount of venom provided is standardised according to protein content, which is determined by microspectrophotometry. Larger amounts are available as part of our custom service.
Any aqueous assay-compatible buffer.
Typically they are single-shot (n=2-3) with enough material for a backup. If you do have some left over, they can be frozen at -20 °C and reused. It is best to avoid repeated freeze-thaw cycles, but we recommend no more than three.
Yes, but do not freeze-thaw more than three times.
Our T-VDA™ solutions are supplied in SLAS (formerly SBS) plates, usually Echo-compatible 384-well plates. 384LDV, 96- and 1,536-well plates are also available. Please feel free to enquire about your preferred assay plate.
Although proteins and peptides are known to potentially stick to plastics, they also can stick to other proteins. Therefore, we recommend not using BSA or other blocking proteins unless it is critical for your experiments.
Yes, power weighing hoods are better, but the lyophilised venoms are unlikely to be blown out of the wells in fume hoods or cell culture MBSCs.
Our peptides are manufactured synthetically, mimicking the power of evolution, and do not contain any animal products. They have built in stabilisation and are non-toxic to human cells in culture. Specific data is provided with each product.
See our crop protection page for further information.
A Targeted-Venom Discovery Array™ (T-VDA™) is engineered to maximise the chance of success, even for challenging targets and new mechanisms of action. They are ideal for target identification and validation, and proof of concept or mechanism studies, all the way through to marketed drugs. Venom is fractionated from a collection of 12-15 targeted species, and is supplied purified and freeze-dried in 384-well Echo-qualified plates. There are typically 1-5 peptides per well with up to a 6 % hit rate.
Yes, your T-VDA™ can be used in any biochemical or cell-based assay, like any other compound array. We have found that a fractionated T-VDA™ also performs well in phenotypic assays.
Approximately 30 % snakes, 30 % tarantula, 10 % true spiders, 20 % scorpions, 10 % others (jellyfish, insects, etc.). See our species list for more information.
Customers typically report a 1-6 % hit rate from screening a Venomtech T-VDA™.
Venom peptides designed through our VenomSELECT™ service have been specially selected to avoid the toxic regions and focus on the required activity. They are also fully tested for in vitro safety before going forward to human trials.
Each well may contain between 1 and 5 entities, but the distribution is skewed to the lower end.
Approximately 200 species, which can be fractionated into ~20,000 molecules
Venoms contain a wide range of active peptides that individually act on a very wide range of receptors and targets. Please see our cosmetics page for more information.