Hyper-Raman spectroscopy of non-proteinogenic amino acids.

Autor: Liu TH; Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Meguro, Tokyo, 153-8902, Japan., Okuno M; Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Meguro, Tokyo, 153-8902, Japan. cmokuno@g.ecc.u-tokyo.ac.jp.
Jazyk: angličtina
Zdroj: Analytical sciences : the international journal of the Japan Society for Analytical Chemistry [Anal Sci] 2024 Dec 13. Date of Electronic Publication: 2024 Dec 13.
DOI: 10.1007/s44211-024-00698-1
Abstrakt: We report 532-nm and 1064-nm excited hyper-Raman (HR) spectra of representative non-proteinogenic amino acids, including α-, β-, and γ-amino acids. Different from the common 20 proteinogenic amino acids, natural non-proteinogenic amino acids cannot be incorporated into proteins during translation, while they are indispensable as intermediates in many processes like biosynthesis and neurotransmitters. In 532-nm excited HR spectra, the COO ─ symmetric stretching bands are commonly intense, and the NH 3 + bands are clearly observable. In addition, based on the reported IR and Raman study, we found that some HR bands are IR-active but Raman-inactive. In contrast, HR signals with the 1064-nm excitation are much weaker than the 532-nm excitation. Nevertheless, we observed the COO ─ scissoring band unexpectedly, much stronger than other bands with the 1064-nm excitation. Our results suggest that the electronic resonance effect plays a role in enabling us to detect HR signals in the UV region readily. We expect that this study provides a supplementary reference for HR spectroscopy of natural amino acids.
Competing Interests: Declaration. Conflict of interest: The authors have no conflicts of interest to declare.
(© 2024. The Author(s).)
Databáze: MEDLINE
Externí odkaz: