Flower power inspires drug cell breakthrough

Conventional drug treatments rely on binding to proteins linked to diseases in order to penetrate cells. Peptides, comprising a smaller number of amino acids than do proteins, are more easily broken down.

However the effectiveness of both is limited by sensitivity to high temperature and the possibility of their 3D structures unravelling.

But writing in the Journal of the American Chemical Society, researchers explained how they were able to join the loose ends of peptides and proteins to create rigid versions that were much more stable, improving their cell penetration.

The catalyst for their work was the extraction of the OaAEP1 enzyme from the tropical flower Oldenlandia affinis. This was modified and transferred into bacterial cells with the cultures then grown to mass produce a protein.

Whereas plants can achieve the process naturally, the cyclisation process can be achieved already through much faster chemical means. However the process remains protracted and involves toxic solvents, making it more costly and less sustainable.

Use of a bacterial system reduces cost and complexity, with the benefit too of biologically friendly reagents. 

The OaAEP1 enzyme was applied to the protein DHFR to demonstrate its effectiveness, increasing resistance to heat changes.

Said Dr Simon Tang, Research Associate from the University of Bath’s Department of Life Sciences: “Our new process lets the bacteria do all the work – the result is it’s also cleaner and greener, and because it has fewer steps, it is a lot simpler to do. 

“We’re really excited about the potential applications of this, not only for the pharmaceutical industry but other industries such as the food industry, detergent industry, in biotechnology, and in bioenergy production.”

The researchers have filed a patent for the technique. For further information about the research click here.