Toxins in treatments!

This is really interesting. People usually avoid toxins. Because they cause harm. But what if we can use this harmful nature to kill things we don't want in our body?

Scientists are exactly doing this in some of their research work.

Protein toxins confer a defense against predation/grazing or a superior pathogenic competence upon the producing organism. Such toxins have been perfected through evolution in poisonous animals/plants and pathogenic bacteria. Over the past five decades, a lot of effort has been invested in studying their mechanism of action, the way they contribute to pathogenicity and in the development of antidotes that neutralize their action.

In parallel, many research groups turned to explore the pharmaceutical potential of such toxins when they are used to efficiently impair essential cellular processes and/or damage the integrity of their target cells. 

Important things to consider in these treatments :

Researchers at the University of São Paulo's Ribeirão Preto School of Pharmaceutical Sciences (FCFRP-USP) in Brazil have identified a molecule in the toxin of Brotheas amazonicus that acts against breast cancer cells similarly to a common chemotherapy drug.

Researchers affiliated with the institution are dedicated to cloning and expressing bioactive molecules—such as proteins from rattlesnake and scorpion venom—through projects within the scope of the Center for Translational Science and Development of Biopharmaceuticals (CTS), located at the Center for the Study of Venoms and Venomous Animals (CEVAP) of São Paulo State University (UNESP), in its Botucatu campus.

This work has resulted in the development of a patented CEVAP product called fibrin sealant, a "biological glue" made from serineproteinase extracted from snake venom (such as from Bothrops neuwiedi pauloensis and Crotalus durissus terrificus) and cryoprecipitate rich in fibrinogen extracted from the blood of buffalo, cattle, or sheep.

These components combine in application to form a fibrin network that mimics the natural coagulation and healing processes. The sealant has been studied for use in nerve gluing, treating bone injuries, and restoring movement after spinal cord injuries. It is currently in phase three clinical trials, the final stage of analysis for a new drug before approval.

Recently, researchers cloned and expressed a different rattlesnake serine protease called cholinein-1. This protease has a different amino acid sequence from the gyroxine toxin, which is extracted directly from rattlesnake venom and used in the production of fibrin sealant.

Through heterologous expression in this yeast isolated in France in 1950, the researchers also intend to obtain an endothelial growth factor called CdtVEGF, which was identified in the rattlesnake species Crotalus durissus terrificus.

This growth factor favors the formation of new vessels. If we combine it with colinein-1, we can create an improved fibrin sealant compared to the one being developed at CEVAP, with the possibility of expanding the industrial scale, since it can be obtained through heterologous expression

Through heterologous expression, the researchers also identified two neurotoxins with immunosuppressive action in scorpions. In partnership with colleagues from INPA and UEA, they discovered a bioactive molecule called BamazScplp1 in the venom of the Brotheas amazonicus scorpion that has potential anti-tumor properties.

Test results of the peptide on breast cancer cells revealed a response comparable to that of paclitaxel, a chemotherapy drug commonly used to treat the disease. The peptide induces cell death mainly through necrosis, an action similar to that of molecules identified in other scorpion species.