Researchers Demonstrate Direct Binding of Proprietary Agonists to NR2F6

Regen BioPharma scientists have used a standard biochemical assay to determine if some of its small molecules that have been shown to activate NR2F6 in cells, physically interact with NR2F6 in vitro. The company reports that the experiments indicate that some of Regen's proprietary small molecules bind to, and alter the structure of NR2F6.

The NR2F6 nuclear receptor has been identified as a potentially very important immune cell inhibitor (an immune checkpoint) and cancer stem cell differentiator. The NR2F6 program at Regen aims to identify antagonists of NR2F6 in an effort to unleash the cancer-killing potential of a patient's own immune system as well as identifying agonists which should suppress the immune system in diseases where the immune system is over-activated, such as autoimmunity.

"We have used a well-known biochemical assay, termed a thermal shift assay, to examine whether our drugs in development bind directly to NR2F6. We were delighted to see clear evidence of binding," says Harry Lander, Ph.D., MBA, President and Chief Scientific Officer of Regen. "Although this specific assay does not tell us how tightly the drugs bind, it does tell us that binding is occurring. We are preparing another assay to answer the questions about affinity."

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