Illustration by Xiao Xie
University of California, Berkeley, chemists have devised a novel method to selectively tag tryptophan residues within proteins, potentially leading to the development of new types of drugs and engineered proteins, including those that mediate protein-protein interactions.
Led by Christopher J. Chang and F. Dean Toste, the Berkeley team drew inspiration from nature's synthesis of indole alkaloids, devising an innovative N-sulfonyl oxaziridine reagent. This reagent reacts swiftly and selectively with tryptophan residues, offering a versatile tool for direct protein modification across proteomes without the need for light, electricity, or metal catalysts.
Read the full article of findings published by Chemical and Engineering News.