|United States Of America||Published Application||20180188243||07/05/2018||2015-939|
Wikimedia Commons / https://commons.wikimedia.org/wiki/File:PDB_3d71_EBI.png
FRET (Fluorescence Resonance Energy Transfer) assay measures binding affinities of proteins to visualize their interaction with one another. SUMOs (Small Ubiquitin-related Modifiers) are post-translational modification proteins that are involved in many cellular processes with a distinguished role in transcription inhibition when attached to other proteins. SUMO signaling pathways in conjunction with pathogenesis are vigorously investigated to discover the underlying etiological causes for disease. Currently, biopharmaceutical companies spend $1B to find suitable drug targets. Knowledge of protein-protein interactions will help expedite the drug discovery stage and develop new therapeutic drugs that are cheaper and more effective.
UCR Researchers have developed a novel, quantitative version of the FRET assay to determine accurate and simplified dissociation constant measurements. They were able to achieve this methodology with the SUMO protein and its various interactions with other proteins. The new FRET assay produces consistent and comparable results in less than an hour compared to those of traditional methods that take 12 hours for the same experiment.
quantitative FRET assay, interaction dissociation constant, Kd, SUMOylation E2 ligase, SUMO conjugation, RanGAP1c, contaminate proteins, protein purification, purified protein