1191118-29-2

Upstream product

• 35521-86-9 2,3,4-tri-O-acetyl-6-deoxy-6-fluoro-α-D-galactopyranosyl bromide 
• 638207-70-2 N-fluorenylmethoxycarbonyl-O-(2-acetamido-4,6-O-benzylidene-2-deoxy-α-D-galactopyranosyl)-L-threonine tert-butyl ester 
• 2021-97-8 6-deoxy-6-fluoro-1,2:3,4-di-O-isopropylidene-α-D-galctopyranose 
• 118396-37-5 1,2,3,4-tetra-O-acetyl-6-deoxy-6-fluoro-β-D-galactopyranose 
• 4064-06-6 1,2:3,4-di-O-isopropylidene-α-D-galactopyranose 

Relevant academic research and scientific papers

Synthesis of a Fluorinated Sialophorin Hexasaccharide–Threonine Conjugate for Fmoc Solid-Phase Glycopeptide Synthesis

The decoding of the mechanisms underlying glycan-mediated recognition in disease and health requires access to structurally well-defined oligosaccharides as molecular probes. Owing to their often favourable properties, deoxyfluorosugars have emerged as a promising class of selectively modified carbohydrates for biological and immunological studies. In particular the enhanced metabolic stability and intrinsic immunogenicity of fluorinated carbohydrates has spurred research on their use for vaccine design. Herein, a first total synthesis of an orthogonally protected and fluorinated hexasaccharide–threonine conjugate of the natural sialophorin antigen has been accomplished. Starting from readily available monosaccharide building blocks, the targeted glycosyl amino acid 1 was assembled by a [3+3′]-block glycosylation strategy. Together with its (1→4)-linked regioisomer the glycan mimic can be applied to solid-phase glycopeptide synthesis to access novel sialophorin-derived molecular tools for functional and biomedical studies.

Fluorinated glycosyl amino acids for mucin-like glycopeptide antigen analogues

The aberrant glycosylation profiles of mucin glycoproteins on epithelial tumour cells represent attractive target structures for the development of immunotherapy against cancer. Mucin-type glycopeptides have been successfully investigated as molecularly defined vaccine prototypes for triggering humoral immunity but are susceptible to rapid in vivo degradation. As a potential means to enhance the bioavailabilities of the antigenic structures, hydrolysis-resistant carbohydrate analogues with fluorine substituents at positions C6, C2′ and C6′ were synthesised and incorporated into the tandem repeat sequence of the mucin MUC1. The resulting pseudo-glycopeptides can be used to elucidate the effects of chemically modified antibody determinants on metabolic and immunological properties.

Synthesis of fluorinated analogues of tumor-associated carbohydrate and glycopeptide antigens

Partial structures of tumor-associated mucin glycoproteins are interesting target structures for the development of selective anticancer vaccines. To probe the effect of fluorination on the immunological and metabolic properties of mucin glycopeptides, six novel fluorinated glycosyl-threonine conjugates have been synthesized. The synthesis of the orthogonally protected glycosyl amino acids was achieved using microwave irradiation in key fluorination and glycosylation steps. The 2′-deoxy-2′-fluoro- and 6′-deoxy-6′-fluoro-T antigen building blocks were applied to the synthesis of analogues of MUC1 tandem repeat-glycopeptide antigens via SPPS. Georg Thieme Verlag Stuttgart.