221325-43-5Relevant articles and documents
A novel silyl linker: Motif for side chain tethered approach to solid- phase glycopeptide synthesis
Nakamura, Kazuhiko,Ishii, Akira,Ito, Yukishige,Nakahara, Yoshiaki
, p. 11253 - 11266 (2007/10/03)
In order to facilitate the solid-phase syntheses of protected glycopeptide blocks, we designed a novel silyl linker, which allows the alcoholic side chain (carbohydrate, serine, or threonine) of (glyco-)peptides to link to the solid support. Utilizing this linker, peptide coupling reactions at both the N- and the C-termini were successful. Synthesis of the glycophorin AM fragment corresponding to the N-terminal glycoheptapeptide is demonstrated.
Design and synthesis of silyl ether-based linker for solid-phase synthesis of glycopeptides
Nakamura, Kazuhiko,Hanai, Noriyasu,Kanno, Masayuki,Kobayashi, Aki,Ohnishi, Yuki,Ito, Yukishige,Nakahara, Yoshiaki
, p. 515 - 518 (2007/10/03)
A novel silyl linker was designed to facilitate the solid-phase synthesis of protected glycopeptide blocks. Alcohols (carbohydrate, serine, or threonine) were silylated with trialkylchlorosilane containing the p- nitrophenyl group. The nitro group was reduced and succinylated to give the succinanilic acids, which were attached to the glycine-preloaded resin via activation with HBTU/HOBt. After elongation of the peptide chain by segment condensation of Fmoc chemistry-based stepwise method, the synthesized glycopeptides in the protected form were split from the resin by fluoridolysis.