New allyl ester linker and solid-phase block synthesis of the serglycin core region.
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).
Nakahara
Y
Y
The Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
Ando
S
S
Ito
Y
Y
Hojo
H
H
Nakahara
Y
Y
D002240:Carbohydrate Sequence; D004952:Esters / Q000737:chemistry; D007202:Indicators and Reagents; D009904:Optical Rotation; D011509:Proteoglycans / Q000138:chemical synthesis* / Q000737:chemistry; D033921:Vesicular Transport Proteins
D004952:Esters; D007202:Indicators and Reagents; D011509:Proteoglycans; D033921:Vesicular Transport Proteins; C075430:serglycin