Scientists describe an improved, cost-efficient method to isolate membrane proteins, a class of proteins that are the targets of more than 60% of approved therapeutic drugs.
Studying proteins in detail requires them to be separated away from thousands of other proteins and lipids (molecular fats) present in the cell. This purification of proteins is essential to gain structural information, which is used to design target drugs. But purification of membrane protein has been a major hurdle that often limits scientific advances. So, pharmacological and medical applications are also being refrained by these limitations.
The article published in Nature Protocols, results from collaboration between scientists at the University of Leeds and University of Birmingham.
In order to overcome these limitations, scientists at the University of Leeds and University of Birmingham have developed a new technology using a polymer called SMA (Styrene maleic acid). This polymer is already being used in plastics of car dashboards and increasingly in cosmetics, but its application to the scientific and medical field is new.
The main advantage of SMA polymer is that it cuts proteins out in their natural environment, which is essential to keep the function of the proteins intact.
Dr Vincent Postis, one of the first authors of this publication said: “Our technique uses SMA-like a ‘cookie cutter’ to extract membrane proteins in its fully folded state held together by surrounding membrane lipids. It allows researchers to study the protein readily following isolation. This method enables the purification of a range of membrane proteins, from small to very large, that was for many years deemed almost impossible by many scientists.”
Purifying proteins in its naturally folded state allows scientists to get insights into the 3D details of the protein structure. Insights into the detailed shape of the proteins are essential for targeted drug design – just like designing a key to fit the lock.
Currently, scientists try many different target drugs and hope it will fit the target protein. But with this new technique, we can understand the shape of the keyhole (3D structure of target protein) and then design the key (target drug) that fits.
This new technique may prove to be particularly important with the current emergence of antibiotic resistant ‘superbugs’. Increased antibiotic resistance has urged the identification of new and efficient drugs. This new method has the potential to enable scientists to carry out research to do exactly that.
The full article can be accessed by clicking the link below but is not open access, so please contact the authors to request a copy.