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Snake venom may be key to treating high blood pressure

Brazilian researchers have discovered two new peptides in snake venom that possess significant potential to treat high blood pressure. The peptides were found in the venom of two snake species native to Brazil.

In two recently published studies, experts analyzed the venom of the lancehead pit viper Cotiara (Bothrops cotiara) and the South American bushmaster (Lachesis muta).

Untapped potential 

The research highlights the untapped potential of venoms, as well as the biotechnological capabilities of these natural substances.

Alexandre Tashima, the principal investigator of both studies, is a professor at the Federal University of São Paulo’s Medical School (EPM-UNIFESP).

“Venoms never cease to surprise us. Even with so much accumulated knowledge, fresh discoveries are possible, such as unpredictable fragments that are parts of known proteins. Despite all the available technology, a great deal remains to be studied in these toxins,” said Professor Tashima. 

Cotiara venom

One such discovery is the peptide named Bc-7a, found in B. cotiara’s venom. While it originates from a protein causing hemorrhaging in prey, it is closer in functional terms to peptides such as those used in captopril, a drug that lowers blood pressure by inhibiting the activity of angiotensin-converting enzyme (ACE).

Overall, the researchers identified 197 peptides in Cotiara – 189 of which are new discoveries. This is a significant increase from 73 peptides found in the same snake’s venom in 2012.

According to the researchers, the difference is due to the use of faster and more sensitive equipment than was available a decade ago, and to the larger number of peptide sequences now available in databases.

South American bushmaster 

The study on bushmaster venom from L. muta, published in the journal Biochemical and Biophysical Research Communications, has identified 151 peptides, with 126 previously unknown. 

Among these, the metalloproteinase-derived peptide Lm-10a stands out. This peptide, a fragment of a hemorrhagic toxin, inhibits ACE and shows potential as a future drug ingredient to treat hypertension.

The analysis suggested that Lm-10a from both L. muta and Bc-7a from B. cotiara resulted from fragmentation processes during venom maturation in the snake’s venom gland and that many more peptides could be obtained from the toxins.

Further research is needed 

While these findings are promising, Professor Tashima emphasized the need for further research to fully understand and harness the potential of these peptides. 

“Despite advances in sequencing technology and the production of large amounts of data in recent years, much remains to be discovered about the vast universe of peptides and their biological roles,” said Tashima. “We must take advantage of our good fortune in being able to study these species, many of which will be extinct before they’ve even been discovered.”

The research is published in the journal Biochimie.

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