Researchers at the University of Bath have drawn inspiration from nature to create a groundbreaking tool that could revolutionize the development of pharmaceutical treatments. The innovative approach focuses on utilizing small proteins known as ‘peptides’ instead of traditional small molecule drugs to disrupt protein interactions more effectively.
One of the challenges with peptides and proteins is their vulnerability to unraveling and sensitivity to high temperatures, making them less viable for drug development. The scientists at the University of Bath overcame this hurdle by creating rigid “cyclic” proteins and peptides. By joining the loose ends of these molecules together, they improved heat and chemical stability and enhanced the ability to deliver them into cells.
The researchers employed an enzyme called OaAEP1 from the Oldenlandia affinis flower, a tropical plant. They modified the enzyme and introduced it into bacterial cells for mass production of cyclic proteins. This process is more sustainable, environmentally friendly, and cost-effective compared to traditional methods.
The bacterial OaAEP1 technology was applied to a protein called DHFR, demonstrating increased resistance to temperature changes while maintaining normal functionality. Professor Jody Mason from the University of Bath highlighted the potential of this flower-inspired technique in drug discovery, leveraging the natural defense mechanism of the Oldenlandia plant to produce cyclic proteins.
Dr. Simon Tang, a Research Associate at the University of Bath, emphasized the broader applications of the process in various industries beyond pharmaceuticals, including food, detergent, biotechnology, and bioenergy production. The researchers are optimistic about the implications for creating cleaner, greener, and more cost-effective drug development methods.
