Vibrational spectra and crystal structure of the di-amino acid peptide cyclo(L-Met-L-Met): comparison of experimental data and DFT calculations

Experimental Raman and FT‐IR spectra of solid‐state non‐deuterated and N‐deuterated samples of cyclo(L‐Met‐L‐Met) are reported and discussed. The Raman and FT‐IR results show characteristic amide I vibrations (Raman: 1649 cm−1, infrared: 1675 cm−1) for molecules exhibiting a cis amide conformation. A Raman band, assigned to the cis amide II vibrational mode, is observed at ∼1493 cm−1 but no IR band is observed in this region. Cyclo(L‐Met‐L‐Met) crystallises in the triclinic space group P1 with one molecule per unit cell. The overall shape of the diketopiperazine (DKP) ring displays a (slightly distorted) boat conformation. The crystal packing employs two strong hydrogen bonds, which traverse the entire crystal via translational repeats. B3‐LYP/cc‐pVDZ calculations of the structure of the molecule predict a boat conformation for the DKP ring, in agreement with the experimentally determined X‐ray structure. Copyright © 2009 John Wiley & Sons, Ltd. Solid‐state non‐deuterated/N‐,O‐ deuterated of‐resonance Raman and FT‐IR data are reported for the cis amide peptide cyclo(L‐Met‐L‐ Met). The experimentally attained X‐ray crystallographic structure is compared and contrasted with that obtained via DFT (B3‐LYP/cc‐pVDZ) calculations. Normal coordinate analysis is used to make vibrational band assignments.