Chemical reactivity hotspots on protein landscape
The surface of protein offers a rich landscape of functional groups. Chemical tools for site-specific labeling of these functionalities is desired for their wide range of applications in understanding biological interactions, ligand discovery, disease diagnosis, and biophysical investigations. Typically, these diagnostic tools can be accessed by the derivatization of nucleophilic side chains in the case of unmodified proteins.
Our research group is investing efforts to develop chemo- and site-selective chemical methodologies for labeling of proteins. Here, the first step involves the development of transformations that would be efficient in controlled reaction conditions such as aqueous buffer, neutral pH and room temperature. The most critical challenge relates to the identification of principles that would allow us to generate reactivity biases at specific sites of the protein. Our ongoing efforts in this direction will be discussed in the presentation.