| Research Abstract |
Glycosaminoglycans (GACs) are classified into two categories having different properties; heparin-type and chondroitin-type. However, glycosyl transfer mechanisms of the first hexosamine residue sorting the GAG into these two categories, are unknown. This fact prompted us to synthesize the proteoglycan probe that could be directly used for the enzymatic glycan elongation in order to elucidate the sorting mechanisms. So far as we know, it has been appointed that the heparin-type of GAG often linked to the hydrophobic and the neighboring acidic regions of the core-peptide. This suggests that the first hexosaminyl transferase recognizes the environment coordinated with the specific peptides to determine the category of GAG. Thus, the tetraosyl oligopeptides composed of GlcA-Gal-Gal-Xyl linking to the hydrophobic and acidic peptides, a partial sequence of the betaglycan, have been selected as the targeted compound to be synthesized. At the beginning of the project, the corresponding tetraosyl hexapeptide was synthesized with liquid phase method. The same type compound was also obtained with the solid support synthesis, of which synthetic protocol led to the successful formation of the corresponding tetraosyl hexadecapeptide. Within the term of this project, the targeted glycosyl oligopeptides were synthesized and proteoglycan synthesis with solid support method was also established.
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