13C-N.M.R. study of the conformation of helical complexes of amylodextrin and of amylose in solution.

Amylose (average d.p. 1000) and amylodextrin (average d.p. 25) have identical 13C-n.m.r. spectra, except for some minor signals from the small amount of alpha-1----6 branch linkages present in amylodextrin. Amylodextrin can be obtained as stable solutions in much higher concentrations than amylose and so requires only 1/100th as many scans to obtain a spectrum comparable to that of amylose. 13C-N.m.r. spectroscopy has been used to study the formation of amylodextrin complexes with organic complexing agents in aqueous solution. A control study using dextran, which does not form helical complexes, showed that, when complexing agents are added, the signals from all of the carbons show a slight downfield shift due to a general solvent effect. In the case of amylodextrin, the addition of increasing concentrations of complexing agent also produced a downfield shift of the signals of all the carbons, but there was a greater shift of the signals for carbons 1 and 4 than for carbons 2, 3, and 6, indicating that something more than a solvent effect was occurring. The cycloamyloses (cyclic alpha-1----4 linked D-glucose oligosaccharides which may be considered as model for an amylose helix) in water have chemical shifts for carbons 1 and 4 that are comparable to those shown by the amylodextrin complexes. It is thus proposed that the formation of a helical complex with amylodextrin results in a change in the conformation of the glycosidic linkage, which is reflected by greater downfield shifts of the signals for carbons 1 and 4, relative to those for carbons 2, 3, and 6. It was observed that differences in the ratio of the downfield shifts of C-1 and C-4 of the different amylodextrin complexes indicate differences in the degree of compactness of the helical structures. A comparison of the 13C chemical shifts of methyl alpha-D-glucoside and methyl alpha-maltoside showed that, for a molecule as small as a disaccharide, there is a conformational change about the glycosidic linkage when complexing agents are added.