Development of the Direct Deuteration Method for Amino Acids and Characterization of Deuterated Tryptophan.

ABSTRACT: Proteins and peptides are vital biomolecules, and deuterated amino acids are increasingly applied in areas such as drug discovery, metabolic tracing, and neutron scattering studies. In this study, we performed deuteration on all 20 proteinogenic amino acids, including their side chains, and established efficient methods for 13 amino acids. Using a Pt/C-catalyzed hydrogen-deuterium exchange reaction, the reaction parameters were optimized to achieve the selective and stable incorporation of deuterium. In addition, the resulting deuterated compounds, focusing on tryptophan, were characterized in order to assess their physicochemical properties. Because the deuteration reaction caused significant racemization of amino acids, deuterated D/L-tryptophan was isolated using a chiral separation met

SUBMITTER: Shibazaki C 

PROVIDER: S-EPMC12467387 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature