Polar-apolar characteristics and fibrillogenesis of glycosylated collagen.

To find the effect of carbohydrate on collagen fibrillogenesis, type I skin collagen was glycosylated by glycosyltransferase, and type II cartilage collagen was deglycosylated by glycosidase. The secondary structures remained unchanged, but the tertiary structures were altered, as shown by increased TNS fluorescence of the bound probe in the glycosylated form. Since TNS binds preferentially to the hydrophobic region of a protein molecule, glycosylation caused an apparent increase in the available hydrophobic sites for the dye. Glycosylation also resulted in a longer lag time and a slower growth rate of fibrillogenesis, although the amount of fibrils formed was unchanged. Deglycosylation resulted in a shorter lag time and an increased rate of fibrillogenesis. Neither glycosylation nor deglycosylation changed the stability of the molecule, as was evident from the melting temperature.