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The spatio-temporal organization of proteins within the cell membrane canaffect numerous biological functions, including cell signaling, communication,and transportation. Deviations from normal spatial arrangements have beenobserved in various diseases, and better understanding this process is a keystepping-stone to advancing development of clinical interventions. However,given the nanometer length scales involved, detecting these subtle changes hasprimarily relied on complex super resolution and single molecule imagingmethods. In this work, we demonstrate an alternative fluorescent imagingstrategy for detecting protein organization based on a material that exhibits aunique photophysical behavior known as aggregation induced emission (AIE).Organic AIE molecules have an increase in emission signal when they are inclose proximity and the molecular motion is restricted. This propertysimultaneously addresses the high background noise and low detection signalthat limit conventional widefield fluorescent imaging. To demonstrate thepotential of this approach, the fluorescent molecule sensor is conjugated to ahuman epidermal growth factor receptor 2 (HER2) specific antibody and used toinvestigate the spatio-temporal behavior of HER2 clustering in the membrane ofHER2-overexpressing breast cancer cells. Notably, the disruption of HER2clusters in response to an FDA-approved monoclonal antibody therapeutic(Trastuzumab) is successfully detected using a simple widefield fluorescentmicroscope. While the sensor demonstrated here is optimized for sensing HER2clustering, it is an easily adaptable platform. Moreover, given thecompatibility with widefield imaging, the system has the potential to be usedwith high-throughput imaging techniques, accelerating investigations intomembrane protein spatio-temporal organization.

Detecting disruption of HER2 membrane protein organization in cell membranes with nanoscale precision