Jul 31 2010
A new fluorescent biosensor, called, G protein-coupled receptors (GPCR) biosensor has been developed by the researchers at Carnegie Mellon University. This biosensor will assist in evolving a vital category of drugs that would target the GPCR’s.
According to Jonathan Jarvik, leader of the research team, and professor of Carnegie Mellon who developed the biosensor, estimate that currently only 30% of the drugs available in the market seek GPCRs and some of the most recurrently used drugs belong to this category. , as they play a crucial role inside a cell’s chemical communication circuits, which control imperative functions such as cognition, mood, memory, inflammatory response, digestion and lung and heart functions. The GPCRs in the cell membrane interact with hormones and neurotransmitters, the molecules that are in charge of cellular communication. When one of the molecules runs into a receptor, it transmits a signal along the cell membrane, which in turn starts a response. Once this is done, the receptor departs from the cell membrane and enters the core of the cell.
The researchers used a novel technology named fluoromodules for developing the biosensor. Fluoromodules, patented by the University’s Molecular and Biosensor Imaging Center (MBIC), are devices that consent scientists to regulate the actions of a protein unit present in the living cells endlessly. These probes consist of a non-fluorescent dye called fluorogen and fluorogen-activating protein (FAP). The fluorogen is preset onto the FAP which in turn latches on to the protein molecule in study. This union helps the researchers to locate the protein and analyze its activity as they glow brightly. The fluorescence can be restricted by the addition or deletion of fluorogen, making it highly valuable in comparison to other fluorescent proteins. To establish the exact time when the GPCR leaves the cell membrane, the researchers used an FAP connected to a beta2 adrenergic receptor (â2AR), found in the brain, lung, heart and other tissues. The fluorogen immediately tagged on to the FAP-GPCR combination and gave out vivid luminescence, which muted when the receptor on activation left the cell membrane. The researchers are positive that this system can be used on other receptors and proteins and are presently trying to broaden its utility value.
The research was sponsored by the National Institutes of Health (NIH), and this study was published in the Journal of Biomolecular Screening in June 2010.