Effective therapeutics have been a large component of creating a healthier world population. Medications, such as insulin, developed from therapeutic proteins are essential to the health and safety of many throughout the nation and the world. Many of these medications are derived from a process known as glycosylation, the joining of proteins and sugars. Glycosylation is necessary in such therapeutics because the sugar structures attached to proteins enable the proteins to remain stable and continue functioning properly. However, until recently, the method used to study and create the biosynthetic pathways and resulting structures of glycosylation, involved a highly complex and time-consuming process that utilized mammalian cells.
Researchers at Northwestern University have recently developed a method of creating cell-free systems to study the biosynthetic pathways that lead to the process of the glycosylation of proteins. This new development, known as GlycoPRIME reduces both the time and resources required to study the pathways of glycosylation. As mentioned, the original process involved the growth of mammalian cells which naturally produce glycosylated proteins. However, this took a prolonged period of time and was highly complex, thus reducing the amount and types of proteins that could be created.
Prior to the creation of GlycoPRIME, researchers at Northwestern had discovered cell-free systems to produce certain proteins, however all of these systems were not able to create glycosylated proteins without the use of reengineered living cells. GlycoPRIME, developed by Weston Kightlinger, involves the creation of enzymes that can “modularly build sugars for protein therapeutics” (Ayshford). These enzymes are then studied to understand which of these contribute to the growth of necessary sugars.
After discovering the process, Kightlinger has been able to create 37 various biosynthetic pathways leading to glycosylation. Within these pathways, 23 sugar structures have been created. However, the most significant finding of his studies thus far is that 18 of these structures had not been joined to proteins in the past. Thus, GlycoPRIME has shown researchers a new method of creating glycosylated proteins that can be used in the development of necessary medications and vaccines. Additionally, researchers have understood the importance that this process will hold in their understanding of the true function of various sugar structures. By enabling scientists to closely examine specific types and forms of such structures, GlycoPRIME will help researchers understand the best structures to continue researching and creating to advance their specific studies within therapeutics. Thus, this new process reveals the connections between the studies of AP Biology concerning protein growth and development with the real world application of finding treatments for common diseases.
This research has the potential to create a meaningful impact in the world of medication and health systems in the future. Thus far, this process has been used to develop a vaccine to trigger the immune system. Additionally, it has been used as a method of stabilizing proteins during their circulation in the human body. As this process continues to advance, researchers at both Northwestern and other research institutes hope to develop vaccines derived from glycosylated proteins that can impact only certain parts and systems of the human body. There are also opportunities for GlycoPRIME to impact the world of biomanufacturing by creating compact and efficient methods of providing medications and vaccines in areas with limited resources.
Thus, the development of GlycoPRIME holds significant impacts in the world of both medication and medical research that will contribute to the growth and improvement of health systems throughout the world.