Daniel Nomura, Ph.D.
University of California, Berkeley
NIEHS-funded researchers have developed a method, using probes, to map the reactivity of environmental chemicals across the proteome, the entire set of proteins in a body. According to the researchers, understanding the direct chemical-protein interactions of environmental chemicals may inform how molecules interact in the body and shed light on causes of disease.
By mapping the reactivity of the amino acid cysteine, they were able to show that certain environmental chemicals, including monomethylarsonous acid, a metabolite of arsenic, and pesticides such as chlorothalonil, react with a set of previously unrecognized protein targets that play key roles in metabolism.
The researchers focused on chemicals in the environment known as electrophiles, positively charged or neutral atoms or molecules that are attracted to an electron-rich site. These chemicals can react with certain regions of proteins, potentially leading to protein dysfunction and adverse health effects.
Citation: Medina-Cleghorn D, Bateman LA, Ford B, Heslin A, Fisher KJ, Dalvie EC, Nomura, DK. , DK. 2015. Mapping proteome-wide targets of environmental chemicals using reactivity-based chemoproteomic platforms. Chem Biol 22(10):1394-1405.