Site-specific incorporation of isotopically labeled oxygen atoms in peptides and proteins facilitates a number of biophysical studies, including some of those employing advanced vibrational spectroscopy or mass spectrometry techniques. Here, we present a general method for installing a given oxygen isotope in a specific amide bond in a protein backbone. This approach allows for late-stage functionalization of derivatized peptides or proteins in such a way that oxygen-16, -17, or -18 isotopes can be incorporated into a common precursor with minimal purification required to obtain pure material. Additionally, this chemistry can also be applied to produce isotopically labeled asparagine or glutamine sidechains. Applications to small model systems will be described.

Site-specific isotopic labeling of peptides and proteins for biophysical studies

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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