2023-12-12 17:00:00
The researchers used an enzyme from the flower of Oldenlandia affinis, which uses cyclic peptides to defend itself once morest predators. Credit: Peter Warren Kerry Taylor-Smith Meteored United Kingdom 12/12/2023 – 6:00 p.m. 5 min
Nature is often the perfect muse, and scientists at the University of Bath have that Flower power used to develop a new tool that will help new pharmaceutical treatments more environmentally friendly, cleaner and more cost-effective to produce.
Drug treatments are often tied to the Proteinsdie an Diseases are involved, and block their activityone Symptoms to alleviate or treat the disease. Researchers at the University of Bath’s Department of Life Sciences have developed a method to join the ends of proteins together, making them more stable and able to penetrate cells more easily.
Peptides and proteins
Traditional small molecules, which typically target drugs, are not suitable for blocking protein-protein interactionsso the pharmaceutical industry has turned its attention to the use of small proteins called peptides.
Peptides and proteins work in similar waysbut they are not always very good medicines because their three-dimensional structures can crumble, them sensitive to high temperatures and it can be difficult to get them into the body’s cells.
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“Proteins and peptides are promising drug candidates“But a major hurdle in developing new therapeutics is producing enough to reach patients without incurring astronomical costs,” says research associate Dr. Simon Tang.
Our new process leaves all the work to the bacteria.
Researchers have found a way to overcome this problem; Proteins and peptide strands usually have a beginning and an end, and by tying these loose ends together they created very rigid “cyclic” proteins and peptideswhich have better chemical and thermal stability and can penetrate cells more easily.
They took that OaAEP1 Enzymewhich consists of a small purple flower called Akin to Oldenlandwhich grows in the tropics, modified it before transferring it into bacterial cells; A protein was mass-produced using bacterial cultures and at the same time connected the ends in a single step.
Oldenland related, #Rubiaceaefound along the eastern coast of Madagascar (Tropicos), but also found in the NAP #Bongolava_maintso #Sofia Region @TeamKMCC pic.twitter.com/qx3nqgCncI
— Hajanirina November 26, 2018
“Proteins and peptides are generally quite sensitive to heat, but cyclization makes them much more robust,” explains Professor Jody Mason. “The Oldenlandia plant produces cyclic proteins naturally as part of one Defense mechanismto deter predators. We have this one Blumen-Superpower “By modifying OaAEP1 and combining it with existing bacterial protein production technology to create a truly powerful tool that will aid drug discovery.”
occupied by bacteria
Plants do this naturally, but it is slow and not very productive. Cyclization can be done chemically (by isolating the enzyme and mixing several reagents in a test tube), but requires multiple steps and toxic chemical solvents.
Using a bacterial system is much simpler and cheaper, increases throughput, uses more biologically sustainable reagents and requires fewer steps. The researchers demonstrated their approach by applying the bacterial OaAEP1 technology to the DHFR protein. They discovered that the connection of the head and tail ends more resistant to temperature changes while maintaining normal function.
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“Our new process leavesthe bacteria do all the work; the result is that it is too cleaner and more environmentally friendly “And because it involves fewer steps, it’s much easier to do,” Tang says. “We are very excited regarding the possible applications of this processnot only for the pharmaceutical industry, but also for other industries such as food, detergents, biotechnology and bioenergy production.”
Source note:
Simon Tang, T. M.; Mason. J. M.; Intracellular Application of an Asparaginyl Endopeptidase for Producing Recombinant Head-to-Tail Cyclic Proteins. JACS Au. (2023).
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#superpower #flowers #paves #drug #treatments
