Indexed on: 27 Jul '01Published on: 27 Jul '01Published in: Bioscience, biotechnology, and biochemistry
The prototype glycopeptidyl fragments of serglycin, a proteoglycan with the characteristic peptide sequence of repeating L-seryl-L-glycine, were synthesized by a convergent method involving block condensation on a solid support. In order to facilitate detachment of the protected glycopeptides from the resin, a new allyl ester type of linker, which is cleavable by Pd(O)-catalysis, was designed and used in combination with the commercial acid-labile Sieber amide resin for the solid-phase synthesis. Glycopeptide blocks consisting of [O-(2,3,4-tri-O-acetyl-D-xylosyl)-L-seryl-L-glycine]n (n = 1 - 8) were produced in good yields. Block condensation in a solution was also successful to synthesize up to the hexadecapeptide (n = 8).