還元的重水素化反応を用いる重水素標識アミノ酸の合成研究

概要

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The NMR techniques provide realistic depiction of the structure of proteins in environments similar to those in which they carry out their functions. However, the larger number of signals and the line widths of the signals make NMR spectra of larger proteins more difficult to analyze. The most effective approach to overcoming this problem is stable-isotope labeling of the target proteins. Especially, stereoselective deuteration of only one of the diastereotopic methylene protons or methyl groups of amino acid side-chains is essential for obtaining their precise structural information. In this review, an overview of the recent progress in the synthetic studies on regio - and stereoselectively deuterium - labeled amino acids is described: 1) stereo-divergent synthesis of L-threo- and L-erythro-[2,3-D_2]amino acids using optically active diketopiperazine as a chiral template, 2) stereoselective deuterium-labeling of diastereotopic methyl and methylene protons of L-leucine, and 3) stereo-divergent synthesis of (2S,3S,4R,5R)- and (2S,3S,4R,5S)-[3,4,5-D_3]proline depending on the substituent of the γ-lactam ring.
東海大学の論文
2001-03-30