What is it about?
Enantiomeric amino acids have specific physiological functions in complex biological systems. Systematic studies focusing on the solid-state properties of D-amino acids are, however, still limited. To shed light on this field, structural and spectroscopic studies of D-alanine using neutron powder diffraction, polarized Raman scattering and ab initio calculations of harmonic vibrational frequencies were carried out. Clear changes in the number of vibrational modes are observed as a function of temperature, which can be directly connected to variations of the N—D bond lengths. These results reveal dissimilarities in the structural properties of D-alanine compared with L-alanine.
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Why is it important?
This work is motivated by the fact that D-Amino acids, the enantiomers of L-amino acids, are increasingly being recognized as physiologically active molecules as well as potential biomarkers. Nonetheless, the solid-state properties of the two enantiomers have not been fully investigated to date.
Perspectives
From the changes in hydrogen bond geometry, and consequent differences in dynamical behavior reported herein, one may conclude that the respective modes of binding of D-Alanine when compared with L-Alanine will differ. Thus affecting metabolic processes in humans.
Professor Heloisa Bordallo
University of Copenhagen
Read the Original
This page is a summary of: Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers, IUCrJ, January 2018, International Union of Crystallography,
DOI: 10.1107/s2052252517015573.
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