In a groundbreaking discovery, scientists at the University of Bath have harnessed the power of flowers to create a revolutionary tool that will transform the production of pharmaceutical treatments. This new method promises to be more ecological, cleaner, and cost-effective.

Peptides and Proteins: The Key to Medical Breakthroughs

Traditional small molecules used in drugs are not effective in blocking protein interactions. As a result, the pharmaceutical industry has turned its attention to peptides, which are small proteins. However, peptides are not always ideal for medicinal purposes due to their fragile three-dimensional structures, sensitivity to high temperatures, and difficulty in penetrating cells.

«Proteins and peptides show great potential as drug candidates, but the challenge lies in producing enough material to reach patients without incurring exorbitant costs,» explains Simon Tang, a researcher at the University of Bath.

Fortunately, the scientists at the University of Bath have developed a groundbreaking solution. By utilizing an enzyme derived from the Oldenlandia affinis flower, they have successfully created «cyclic» proteins and peptides that are more stable, resistant to heat, and easier to introduce into cells.

Unlocking Nature’s Potential with Bacterial Technology

While plants naturally produce cyclic proteins, the process is slow and inefficient. Chemical cyclization, achieved by isolating the enzyme and using various reagents, is also possible but requires multiple steps and toxic solvents.

The researchers at the University of Bath have taken a different approach by harnessing the power of bacteria. They modified the enzyme obtained from the Oldenlandia affinis flower and transferred it to bacterial cells. By growing bacterial cultures, they were able to mass-produce the desired proteins and peptides while simultaneously joining their ends in a single step.

«The cyclization process makes proteins and peptides much more robust. The Oldenlandia plant naturally produces cyclic proteins as a defense mechanism against predators,» explains Professor Jody Mason, one of the researchers involved in the study.

This innovative method not only simplifies the production process but also reduces costs and environmental impact. It opens up possibilities not only in the pharmaceutical industry but also in sectors such as food, detergent production, biotechnology, and bioenergy.

The researchers have successfully demonstrated the effectiveness of their method by applying it to the DHFR protein. Joining the ends of the protein increased its resistance to temperature changes while maintaining its normal function.

«Our new process allows bacteria to do all the work, making it cleaner, more environmentally friendly, and easier to execute,» says Tang. «We are incredibly excited about the potential applications of this technology in various industries.»

With this groundbreaking discovery, the future of pharmaceutical treatments looks brighter than ever. The use of flower-derived enzymes and bacterial technology has paved the way for more sustainable, cost-effective, and efficient drug production.

News reference:

TANG, T. M. S.; MASON, J. M. Intracellular Application of an Asparaginyl Endopeptidase for Producing Recombinant Head-to-Tail Cyclic Proteins. Journal of the American Chemical Society Gold (JACS Au), 2023.