Frontiers in Chemistry and Chemical Engineering
Prof. Backus received her B.S. in Chemistry and B.A. in Latin American Studies from Brown University in 2007. She conducted undergraduate research in inorganic chemistry at Brown in the laboratory of Dr. Amit Basu on the synthesis and characterization of metal coordinating 1,2,3-triazoles. As part of her undergraduate education, she also conducted research in the laboratory of Dr. Tarun Kapoor at Rockefeller University. As a 2007 Rhodes Scholar and an NIH Oxford Cambridge Scholar, her Ph.D. in Organic Chemistry was conducted jointly in the laboratories of Dr. Benjamin Davis (Oxford) and Dr. Clifton Barry (NIH, NIAID). Her doctoral research focused on the synthesis and application of trehalose-based chemical probes to label and image Mycobacterium tuberculosis. In 2012 Dr. Backus completed her doctorate and began an NIH postdoctoral fellowship at The Scripps Research Institute in the laboratory of Prof. Benjamin Cravatt. At TSRI she developed chemical proteomics platforms to conduct covalent fragment-based screening at cysteine and lysine residues proteome-wide. She has been recognized with a number of prestigious awards including the Packard Fellowship, NIH New Innovator, Beckman Young Investigator Award, Ono Pharma Foundation Breakthrough Science Initiative Award, and Darpa Young Faculty Award. Her research focuses on the development of new chemical tools and chemical proteomics methods to study and manipulate the human immune system.
Cysteine is a unique amino acid, distinguished by its nucleophilicity and sensitivity to oxidative modifications. As a result of this privileged chemistry, cysteine-reactive molecules have emerged as high value tools for functional biology and drug development applications. Exemplifying the importance of these molecules, the recently FDA-approved drug Sotorasib functions by covalently modifying the Gly12Cys oncogenic form of KRAS, a protein long thought to be undruggable. Thus, there is widespread interest in the discovery of new ligandable (potentially druggable) and redox sensitive cysteine residues. Cysteine chemoproteomic platforms, including those from our group, are highly enabling technology increasingly used for the discovery of such high value cysteines. However, a key bottleneck in these pipelines is the absence of a priori insight into the likely functionality of identified cysteines. Here, I will present our group's innovative function-centric chemoproteomic platforms that are tailored to identify functional, redox sensitive, and therapeutically relevant cysteine residues. I will also discuss our ongoing efforts to delineate cysteine-specific drivers of stress granule formation.