Spectroscopic FTIR and NMR study of the interactions of sugars with proteins.

FTIR and NMR spectra were measured in parallel for specific two-components mixtures of various proteins with different sugar molecules, such as arabinose, glucose, and sucrose. In the FTIR spectra of arabinose with some of these proteins, the bands assigned to the vibrational modes of the CH and COH groups disappeared, and new ones, related to an arabinose-protein CN mode, appeared. Similar changes were observed in the FTIR spectra of lyophilized mixtures of arabinose with different amino acids. In additional FTIR spectra, measured for other protein-sugar mixtures, the bands correlated to the ring modes of arabinose, in the range 1150-1000 cm, disappeared, and two new very strong narrow bands became dominant, indicating ring opening or some kind of arabinose decomposition. Contrary to the prevailing opinion that complexes between sugars and proteins are formed mainly by hydrogen bonds, the IR and NMR spectra of the sugar-protein mixtures studied here suggest that significant chemical reactions also take place between the interacting sugar and the protein. Two types of sugar-protein chemical reactions can be distinguished on the basis of these IR spectra, leading to the formation of a new CN bond and to the decomposition of sugar skeletal bonds. The new IR bands suggest that the latter reaction results in the formation of new bonds, which are related to new polyether moieties. These results highlight the often ignored non-specific chemical reactions that take place between sugars and proteins, and demonstrate that the simultaneous application of FTIR and NMR spectroscopic analyses can detect and further characterize these types of sugar-protein interactions.