Selective modification of biomolecules provides scientists with an effective tool for a multitude of bioanalytical, therapeutic, biological and bioengineering applications. However, chemical strategies that can target a particular functional group at a single site in the presence of reactive amino acid side chains on protein surfaces are limited. In this seminar, I will introduce the research in the Raj Lab at Emory. First, I will focus on our efforts to develop novel multicomponent bioconjugation approaches for selective labeling of proteins. This method does not require any genetic engineering of the protein target and protection of the side chains of other amino acids. The resulting bioconjugation reaction leads to the formation of a highly stable C-C bond at the site of the conjugation. This method is employed for labeling monomethyl lysine containing posttranslational modifications (PTMs) on proteins with various cargoes. The dysregulation of monomethyl lysine PTMs has been linked to a variety of different biological malfunctions, yet the chemical methods for selective detection of monomethyl lysine PTMs are still lacking. I will explain how our method can be used for detecting monomethyl lysine PTMs. Second; I will focus on our efforts to develop chemical tools for capturing the protein partners of mono- and di-methyl lysine PTMs. This research could lead to the discovery of novel protein biomarkers and new therapies.

Chemical tools for selective recognition of posttranslational modifications and their protein partners

ACS Fall 2021

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