Protein-protein interactions are the core of many intracellular and extracellular biological functions.  Monitoring and potentially biasing these activities in real time is of great importance.  Robust, versatile, environmentally-sensitive fluorophores such as 4-N,N-dimethylamino-1,8-naphthalimide (4-DMN) can be invaluable tools for reporting on protein-protein interactions.  Presented is a strategy for site-specific labeling of efficiently expressed mutant cytokines which will allow for the ultimate goal of further deconvoluting the complexities of cellular signal transduction.  Also presented in a complimentary context, is a new robust and efficient strategy for development of divalent receptor cytokines. Divalent cytokine ligands have been previously shown to bias protein-protein interactions among cell-surface receptors by sequestering HER3 receptors and preventing them from forming potentially cancerous heterodimers with HER2 receptors.  The data presented here will be highly beneficial for understanding extracellular communication and its role in observed phenotypes within a cell, which is of great interest to scientists, and the medical community.

New chemical biology tools for detecting/controlling protein-protein interactions in extracellular communication networks

243rd National Meeting (2012)

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