120173-57-1

Basic information

• Product Name: FMOC-SER(GALNAC(AC)3-ALPHA-D)-OH
• Synonyms: FMOC-SER(AC3ACNH-ALPHA-GAL)-OH;FMOC-SER(GALNAC(AC)3-ALPHA-D)-OH;FMOC-SERINE(GALNAC(AC)3-ALPHA-D)-OH;FMOC-L-SER(ALPHA-D-GALNAC(AC)3)-OH;FMOC-L-SER(TNAC4)-OH;GALNAC L-SERINE;N-ALPHA-FMOC-O-BETA-(2-ACETAMIDO-2-DEOXY-3,4,6-TRI-O-ACETYL-ALPHA-D-GALACTOPYRANOSYL)-L-SERINE;N-ALPHA-FMOC-O-(2-ACETAMIDO-2-DEOXY-3,4,6-TRI-O-ACETYL-ALPHA-D-GALACTOPYRANOSYL)-L-SERINE
• CAS NO: 120173-57-1
• Molecular Formula: C₃₂H₃₆N₂O₁₃
• Molecular Weight: 656.63
• Product Categories: Amino Acid;Carbohydrates & Derivatives;Fluorescent Labels & Indicators;Inhibitors;Protein Kinase Inhibitors and Activators;Glycoamino Acid
• Mol File: 120173-57-1.mol

Chemical Properties

• Boiling Point: 856.8±65.0 °C(Predicted)
• Appearance: /
• Density: 1.39±0.1 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.34±0.10(Predicted)
• CAS DataBase Reference: FMOC-SER(GALNAC(AC)3-ALPHA-D)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-SER(GALNAC(AC)3-ALPHA-D)-OH(120173-57-1)
• EPA Substance Registry System: FMOC-SER(GALNAC(AC)3-ALPHA-D)-OH(120173-57-1)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 120173-57-1(Hazardous Substances Data)

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 83956-40-5 O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-L-serine 
• 67817-41-8 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl chloride 
• 84278-00-2 1,3,4,6-tetra-O-acetyl-2-azido-2-deoxy-D-galactopyranose 
• 68733-26-6 2-deoxy-2-azidogalactopyranose 
• 1772-03-8 D-(+)-galactosamine hydrochloride 
• 108-24-7 acetic anhydride 
• 64-19-7 acetic acid 
• 1391597-84-4 3,4,6-tri-O-acetyl-2-deoxy-2-o-trifluoromethylbenzylideneamino-D-galactopyranosyl N-phenyl trifluoroacetimidate 
• 83025-20-1 3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyltrichloroacetimidate 
• 25878-60-8 D-galactose pentaacetate 
• 1013026-09-9 O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-N-(fluorenylmethoxycarbonyl)-L-serine methyl ester 
• 67817-37-2 3,4,6-tri-O-acetyl-2-azido-2-deoxy-β-D-galactopyranosyl chloride 
• 176207-51-5 (S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-propionic acid 2-(2-methoxy-ethoxy)-ethyl ester 

Downstream Products

• 218291-44-2 C₅₆H₆₆N₄O₂₃ 
• 1448670-81-2 APG(GalNAcα)STAPPA 
• 17041-36-0 3-O-(2-Acetamido-2-desoxy-α-D-galactopyranosyl)-L-serin 
• 120173-61-7 N-(Benzyloxycarbonyl)-L-alanyl-L-prolyl-O-tert-butyl-L-threonyl-O-(2-acetamido-3,4,6-tri-O-acetyl-2-desoxy-α-D-galactopyranosyl)-L-seryl-O-tert-butyl-L-seryl-O-tert-butyl-L-serin-tert-butylester 
• 120204-26-4 L-Alanyl-L-prolyl-L-threonyl-O-(2-acetamido-3,4,6-tri-O-acetyl-2-desoxy-α-D-galactopyranosyl)-L-seryl-L-seryl-L-serin 
• 120173-87-7 L-Alanyl-L-prolyl-L-threonyl-O-(2-acetamido-2-desoxy-α-D-galactopyranosyl)-L-seryl-L-seryl-L-serin 
• 137816-29-6 N^α-(9H-fluoren-9-yl)methoxycarbonyl-O-(3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl)-L-serine pentafluorophenyl ester 

Relevant articles and documents

In vitro synthesis of mucin-type O-glycans using saccharide primers comprising GalNAc-Ser and GalNAc-Thr residues

Mucin-type O-glycosylation of serine or threonine residue in proteins is known to be one of the major post-translational modifications. In this study, two novel alkyl glycosides, Nα-lauryl-O-(2-acetamido-2-deoxy-α-D-galactopyranosyl)-L-serineamide (GalNAc-Ser-C12) and Nα-lauryl-O-(2-acetamido-2-deoxy-α-D-galactopyranosyl)-L-threonineamide (GalNAc-Thr-C12) were synthesized as saccharide primers to prime mucin-type O-glycan biosynthesis in cells. Upon incubating human gastric cancer MKN45 cells with the saccharide primers, 22 glycosylated products were obtained, and their structures were analyzed using liquid chromatography-mass spectrometry and enzyme digestion. The amounts of glycosylated products were dependent on the amino acid residues in the saccharide primers. For example, in vitro synthesis of T antigen (Galβ1-3GalNAc), fucosyl-T (Fucα1-2Galβ1-3GalNAc), and sialyl-T (NeuAcα2-3Galβ1-3GalNAc) preferred a serine residue, whereas sialyl-Tn (NeuAcα2-6GalNAc) preferred a threonine residue. Furthermore, the glycosylated products derived from GalNAc-Ser/Thr-C12 and Gal-GalNAc-Ser/Thr-C12 using cell-free synthesis showed the same amino acid selectivity as those in the cell experiments. These results indicate that glycosyltransferases involved in the biosynthesis of mucin-type O-glycans distinguish amino acid residues conjugated to GalNAc. The saccharide primers developed in this study might be useful for comparing mucin-type oligosaccharides in cells and constructing oligosaccharide libraries to study cell function.

Efficient and reproducible synthesis of an Fmoc-protected Tn antigen

This concise total synthesis of the Thomsen-Nouveau (Tn) glycoconjugate was accomplished using a palladium-catalyzed coupling between the glycosyl donor and Fmoc-protected serine acceptor. This is, to the best of our knowledge, the shortest synthesis reported from galactose for preparing this essential building block for large-scale solid phase peptide synthesis.

Design and synthesis of trivalent Tn glycoconjugate polymers by nitroxide-mediated polymerization

A new synthetic method for preparing Tn glycoconjugate polymers, containing tumor-associated carbohydrate antigens, by controlled living radical polymerization is reported. To mimic the authentic structures of Tn glycopeptide antigens and to explore the controlled living radical polymerization, three tumor-associated carbohydrate antigens (GalNAc, GalNAcα1-O-Ser, and GalNAcα1-O-Thr) were attached to a styrene-type monomer through a diethylene glycol spacer. Under nitroxide-mediated polymerization, controlled living radical polymerization proceeded to afford defined glycopeptide polymers with different Tn densities and compositions. The polydispersity index (PDI) and molecular weights were increased and conversions were decreased upon increasing the concentration of Tn glycoconjugate monomers. The resulting Tn glycoconjugate polymers were characterized by NMR and IR. The spectral data indicate that the Tn glycoconjugate moiety did attach to the polymer chain and Tn glycoconjugate density could be adjusted through the nitroxide-mediated polymerization conditions. The number of Tn units containing in the polymer chains could be estimated by NMR integration. This synthetic approach provides a new and efficient tool for constructing novel Tn glycoconjugate polymers.

COMPOSITIONS AND METHODS OF TREATING CANCER AND INFECTIONS USING BACTERIOPHAGE AND ITS MUTANTS

Provided herein are vaccine composition comprising an antigen conjugated to a capsid, wherein the capsid comprises wild type or native sequence. Provided herein are also vaccine composition comprising an antigen conjugated to a capsid, wherein said capsid comprises at least one mutation, such as a non-natural mutation. Such compositions are useful in the treatment and prevention of pathogenic infections, inflammatory diseases, and neurodegenerative disease, and cancer, among others.

Utilization of bench-stable and readily available nickel(II) triflate for access to 1,2-cis-2-aminoglycosides

The utilization of substoichiometric amounts of commercially available nickel(II) triflate as an activator in the reagent-controlled glycosylation reaction for the stereoselective construction of biologically relevant targets containing 1,2-cis-2-amino gl

Fluorenylmethoxycarbonyl-Protected O-Glycosyl-N-methyl Amino Acids: Building Blocks for the Synthesis of Conformationally Tuned Glycopeptide Antigens

Peptide antibiotics often contain N-methylated amino acids. These N-methylamino components enhance the metabolic stability and strongly influence the conformational behavior of these peptide drugs. N-Methyl-O-glycosyl amino acids, in particular, threonine and serine derivatives, are unknown so far. Fmoc-protected N-methyl-O-glycosyl-threonine and -serine building blocks, including sialyl TN antigens, have been synthesized for the first time by converting the Fmoc-protected O-glycosyl amino acids or their tert-butyl esters into the corresponding oxazolidinones followed by reductive ring-opening. These new components are considered interesting for the construction of modified mucin glycopeptide anti-tumor vaccines with extended biological half-life. Fmoc-protected building blocks of N-methylated O-glycosyl amino acids, inaccessible so far, have been synthesized by the conversion of Fmoc-O-glycosyl amino acids into the corresponding oxazolidines followed by reductive ring-opening. These N-methyl-O-glycosyl amino acids could be used in solid-phase glycopeptide syntheses under particular conditions.

One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid

A series of STn-MUC1 and ST-MUC1 glycopeptides containing naturally occurring and non-natural sialic acids have been chemoenzymatically synthesized from Tn-MUC1 glycopeptide using one-pot multienzyme (OPME) approaches. In situ generation of the sialyltran

Synthesis of Tn/T antigen MUC1 glycopeptide BSA conjugates and their evaluation as vaccines

The tumor-associated mucin MUC1 over-expressed in most epithelial tumor tissues is considered a promising target for immunotherapy. The extracellular part of MUC1 contains a domain of numerous tandem repeats of the amino acid sequence HGVTSAPDTRPAPGSTAPPA, including five potential O-glycosylation sites. In this study, T9 and S15 have been chosen as the positions of glycosylation. The glycopeptides N-terminally equipped with a triethylene glycol spacer were synthesized by microwave-assisted Fmoc solid-phase peptide synthesis. After detachment from the resin and deprotection, the MUC1 glycopeptides were conjugated to bovine serum albumin (BSA). To evaluate the immunological properties, balb/c mice were immunized with these BSA vaccines. Copyright

Chemoenzymatic synthesis of glycosylphosphatidylinositol-anchored glycopeptides

MUC1 glycopeptide was efficiently coupled to glycosylphosphatidylinositol (GPI) derivatives by sortase A (SrtA), verifying that SrtA can accept sterically hindered glycopeptide as substrate for ligation with GPIs. This work has established a practical method for the chemoenzymatic synthesis of GPI-linked glycopeptides.

Microwave-assisted synthesis of fluorescein-labelled GalNAcα1-O-Ser/ Thr (Tn) glycopeptides as immunological probes

Fluorescently labelled glycopeptides containing GalNAcα1-O-Ser/Thr residues provide valuable immunological probes for the development of cancer vaccines. The microwave-assisted automated Fmoc solid-phase synthesis of a series of 5(6)-carboxyfluorescein-labelled GalNAcα1-O-Ser/Thr peptides is described. Lys(Dde)-Gly-Wang polystyrene resin was elongated using Fmoc SPPS with incorporation of several GalNAcα1-O-Ser/Thr residues. Deprotection of the Lys(Dde) then allowed attachment of the 5(6)-carboxyfluorescein label. The synthetic methodology described is flexible and suitably robust enabling the incorporation of three contiguous GalNAcα1-O-Ser residues into the peptide chain. Georg Thieme Verlag Stuttgart · New York.