Development of the Direct Deuteration Method for Amino Acids and Characterization of Deuterated Tryptophan
(2025) In Bioengineering 12(9).- 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... (More)
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 method. Deuterated tryptophan characterization studies confirmed that the photostability was markedly enhanced by deuteration, whereas the acid stability showed no clear isotopic effect. The X-ray crystal structure analyses revealed minimal changes upon the hydrogen-to-deuterium substitution. These results provide a robust platform for the supply of deuterated amino acids, facilitating their application in drug development, structural analysis, and creation of advanced functional biomaterials.
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- author
- Shibazaki, Chie ; Sugiyama, Haruki ; Ueda, Misaki ; Oku, Takayuki ; Adachi, Motoyasu ; Fisher, Zoë LU and Akutsu-Suyama, Kazuhiro
- organization
- publishing date
- 2025-09
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- amino acid, crystal, deuteration, isotope effect, optical isomer
- in
- Bioengineering
- volume
- 12
- issue
- 9
- article number
- 981
- publisher
- MDPI AG
- external identifiers
-
- pmid:41007226
- scopus:105017384883
- ISSN
- 2306-5354
- DOI
- 10.3390/bioengineering12090981
- language
- English
- LU publication?
- yes
- id
- 6e9e7ccf-b444-4b0e-812c-2952539c1840
- date added to LUP
- 2025-11-27 12:45:46
- date last changed
- 2025-12-11 14:14:27
@article{6e9e7ccf-b444-4b0e-812c-2952539c1840,
abstract = {{<p>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 method. Deuterated tryptophan characterization studies confirmed that the photostability was markedly enhanced by deuteration, whereas the acid stability showed no clear isotopic effect. The X-ray crystal structure analyses revealed minimal changes upon the hydrogen-to-deuterium substitution. These results provide a robust platform for the supply of deuterated amino acids, facilitating their application in drug development, structural analysis, and creation of advanced functional biomaterials.</p>}},
author = {{Shibazaki, Chie and Sugiyama, Haruki and Ueda, Misaki and Oku, Takayuki and Adachi, Motoyasu and Fisher, Zoë and Akutsu-Suyama, Kazuhiro}},
issn = {{2306-5354}},
keywords = {{amino acid; crystal; deuteration; isotope effect; optical isomer}},
language = {{eng}},
number = {{9}},
publisher = {{MDPI AG}},
series = {{Bioengineering}},
title = {{Development of the Direct Deuteration Method for Amino Acids and Characterization of Deuterated Tryptophan}},
url = {{http://dx.doi.org/10.3390/bioengineering12090981}},
doi = {{10.3390/bioengineering12090981}},
volume = {{12}},
year = {{2025}},
}