Abstract

Cell surface receptor oligomerization is an attractive target process for drug screening. However, simple but reliable (and thus high-throughput) visualization methods for receptor oligomerization are still lacking. Herein, we report on a new single-construct homo-molecular fluorescence complementation (Homo-FC) probe, which shows strong fluorescence signals by oligomerization of fused receptors in living cells with unexpectedly low background signals. Importantly, this high signal-to-noise ratio was not affected by expression level variations of fused receptors. The Homo-FC probe was developed by optimized flopped fusion of split fragments of superfolder green fluorescence protein and subsequent surface charge engineering. Homo-FC reliably visualized the oligomerization of diverse natural receptors such as GPCR, EGFR, and even cytosolic DAI.

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