It is no longer today that medicine transforms deadly animal venom into medication, and that is exactly what researchers from the Butantan Institute are doing with a toxin from the tarantula Acanthoscurria juruenicola, a species native to the Amazon, as highlighted in an article published in the journal Journal of Proteome Research.
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The group, which also includes researchers from the Federal University of São Paulo (Unifesp) and partners from Brazil and the USA, found a total of 92 proteins, 14 of which are cysteine-rich peptides (CRP), a type of molecule common in spider toxins with effects on ion channels — proteins used as treatment targets and are studied, for example, as potential analgesic agents — and against microorganisms.
Some of these CRPs can cause paralysis in insects. The researchers conducted experiments with small amounts of the venom on crickets and found that this paralysis could last for 24 hours. The idea, then, is to study the substance to the point of developing a biological insecticide.
In previous studies, researchers noted a species of Acanthoscurria with a venom that carries a possible antimicrobial effect, so the expectation is that the currently studied species also has these properties. For this, the group must deepen the analyses.
The scientists noticed a higher concentration of proteins was found in the venom of females, which could be caused by the need for protection of the eggs, thus naturally requiring more venom. “The solution to many problems may be hidden in species that have not yet been discovered or even in others that have been described for a long time, such as this spider”, opine the study’s authors.
Previously, a team from Australia discovered that the venom of the world’s most dangerous spider can help save human hearts. This is the funnel web spider venom protein called Hi1a. This protein works by interrupting a signal that is sent to the cell to die if it does not have enough oxygen, which can happen during an attack or during the removal of the organ for transplantation.
Source: Journal of Proteome Research via FAPESP Agency