Membrane protein interactions that occur on the same cell surface (<i>cis</i>) and across different cells (<i>trans</i>) play essential roles in regulating cellular function. One notable example is the surface interactions between immunomodulatory receptors (IMRs) to initiate and regulate immune responses. The success in modulating these interactions with checkpoint inhibitors such as anti-PDL1/CTLA4 demonstrates the high value in understanding how IMRs interact and the proteins that can effect their functions. A powerful technique for the unbiased assessment of protein-protein interactions or bystander proteins with effector function on the cell surface is protein proximity labeling. A number of enzyme-based strategies have been developed over the last 10 years that either generate a reactive labeling species in proximity to the protein of interest, or physically stamp" neighboring proteins. The success of these approaches has led to the consideration of other chemical-based methods that are smaller in size, can be temporally controlled, and/or can avoid harsh treatment conditions. One notable example is the use of photocatalytic-based transformations whereby protein residues are labeled in the presence of visible light and a photocatalyst to alter protein activity and/or probe cellular function. To this end, we have successfully developed a visible light-activated labeling strategy for temporally-controlled membrane protein proximity labeling. This talk will describe the successful demonstration of this novel labeling technology on different cell types including a two cell, immune synapse system with the end goal of identifying proteins with effector function.

Immunomodulatory receptor profiling via photo-driven labeling of the cell surface

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.