Solid-state NMR spectra of amino acid enantiomers and their relative intensities

Abstract

Under normal experimental conditions in an achiral environment, NMR spectra of enantiomers have chemical shifts and J couplings which are not differentiable. In this work, the reproducibility of spectral intensities for pairs of amino acid enantiomers, as well as factors influencing these intensities, is assessed using ¹³C and ¹⁵N cross-polarization magic-angle spinning (CP/MAS) NMR spectroscopy. Prompted by a recent literature debate over a possible influence of the chirality-induced spin selectivity (CISS) effect on spectral intensities obtained in CP/MAS NMR experiments carried out on enantiomers, a number of control experiments were performed with recycle delays of at least 5T₁. These included the analysis of proton-decoupled Bloch decay solid-state NMR spectra as well as solution NMR spectra where the cross polarization process is absent. Bloch decay and CP/MAS NMR spectra yield the same relative intensities for pairs of enantiomers while solution NMR spectra provide relative intensities closest to unity. Differences of plus-or-minus a few percent in the D/L spectral intensity ratios observed in all solid-state NMR experiments are due to sample preparation (i.e., grinding, particle size, partial amorphization) and limitations on sample purity. As previously described in the literature, more drastic intensity differences on the order of 50% are easily created by ball milling the samples. Finally, apodization is shown to invert the apparent D/L ratio in low signal-to-noise ¹⁵N CP/MAS NMR spectra of aspartic acid enantiomers. In summary, no spectral intensity differences attributable to enantiomerism are identified.

Keywords: Chemical shift; Enantiomer; Reproducibility; Solid-state NMR.