New production methods for stable-isotope labeled amino acids that are suitable for NMR structural study of membrane proteins were identified as necessary for further advances in this field. Phase I aims to evaluate the usefulness of Schoellkopf's lactim alkylation method for commercial L-tyrosine-3-13C, L-leucine-4-13C, and possibly L-threonine-3-13C. Preparation of the requisite labeled moieties are pursued using some new labeled reagents and reactions recently developed. Should the method prove viable, Phase II will develop the preparative steps for other unknown labeled analogs of common proteinogenic amino acids.
The research may result in a new reliable production method for deuterium- or 13C-labeled amino acids that are suitable for NMR study of proteins and metabolic tracers.
