Solid-state vibrational circular dichroism studies on the conformation of an amino acid molecule in crystalline state

Abstract

The present article reviews the results of solid-state vibrational circular dichroism (SD-VCD) measurements on the crystals of amino acids. The investigated series were Ala, Ile, Leu, Phe, Ser, Val, and Thr. Spectra were recorded for the samples containing both D- and L-enantiomers. The molecular conformation in a crystalline state was compared among the series. Molecule optimization of their conformation under intermolecular interactions in crystalline states was revealed. One noteworthy aspect was that some VCD peaks were remarkably enhanced in comparison with the solution states. This fact was rationalized in terms of vibrationally coupled delocalization in a closely stacked pair. In addition, for a molecule with two asymmetric carbons, the signs of the VCD peaks were determined by the interplay between the two chiral centers. Lastly, the roles of the theoretical approach based on density functional theory calculations were described.

Keywords: D-amino acid; Density functional theory; Vibrational circular dichroism.