89077-02-1Relevant academic research and scientific papers
Synthesis of sialyl Lewis X mimetics and related structures using the glycosyl phosphite methodology and evaluation of E-selectin inhibition
Lin, Chun-Cheng,Shimazaki, Makoto,Heck, Marie-Pierre,Aoki, Shin,Wang, Ruo,Kimura, Teiji,Ritzèn, Helena,Takayama, Shuichi,Wu, Shih-Hsiung,Weitz-Schmidt, Gabriel,Wong, Chi-Huey
, p. 6826 - 6840 (2007/10/03)
This paper describes our recent study of glycosyl phosphites for glycosylation reactions, with particular emphasis on the investigation of protecting group and stereochemistry effects on the anomeric reactivity and stereoselectivity, and the application of this methodology to the synthesis of Lewis X (Le(x)), Lewis Y (Le(y)), glycopeptides, and sialyl Lewis X (SLe(x)) mimetics. Both α-O-fucosyl-L-threonine and α-O-fucosyl-(1R,2R)-2-aminocyclohexanol were found to be effective templates for the chemical/enzymatic synthesis of SLe(x) mimetics, and some fucopeptides prepared were 5-10 times more active than SLe(x) as inhibitors of E-selectin.
Solid-phase synthesis of a fucosylated glycopeptide of human factor IX with a fucose-α-(1->O)-serine linkage
Peters, Stefan,Lowary, Todd L.,Hindsgaul, Ole,Meldal, Morten,Bock, Klaus
, p. 3017 - 3022 (2007/10/03)
The chemical synthesis of a glycopeptide with L-fucose directly linked to the hydroxy group of L-serine is reported.Two building blocks containing a protected and an unprotected fucose residue α-glycosidically linked to Nα-Fmoc-Ser-OH were prepared and used in the synthesis of a glycopeptide fragment of the EGF domain of Human Factor IX 55-65.It was demonstrated that both building blocks were completely compatible with the standard Fmoc-based solid-phase peptide synthesis protocol and furthermore that OH protection of the carbohydrate is necessary only during the final acid treatment for cleavage of the glycopeptide from the resin.
