160067-63-0

Basic information

• Product Name: O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N- a-(fluoren-9-yl-methoxy carbonyl)-L-serine
• Synonyms: FmocSer(Ac3-b-D-GlcNAc)-OH ;O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N- a-(fluoren-9-yl-methoxy carbonyl)-L-serine;FmocSer(Ac3--D-GlcNAc)-OH;O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-β-D-glucopyranosyl)-N- α-(fluoren-9-yl-methoxycarbonyl)-L-serine;O-(2-AcetaMido-2-deoxy-3,4,6-tri-O-acetyl-β-D-glucopyranosyl)-N-FMoc-L-serine;2-Acetamido-3,4,6-tri-O-acetyl-2-deoxy-b-D-glucopyranosyl-Fmoc serine;N-[(9H-Fluoren-9-ylMethoxy)carbonyl]-O-[3,4,6-tri-O-acetyl-2-(acetylaMino)-2-deoxy-β-D-glucopyranosyl]-L-serine;FMoc-Ser(β-D-GlcNAc(Ac)3)-OH
• CAS NO: 160067-63-0
• Molecular Formula: C₃₂H₃₆N₂O₁₃
• Molecular Weight: 656.637
• Product Categories: Amino Acids & Derivatives;Carbohydrates & Derivatives;Aromatics;Glycoamino Acid
• Mol File: 160067-63-0.mol
• Article Data: 26

Chemical Properties

• Melting Point: 241-243°C
• Boiling Point: 856.8±65.0 °C(Predicted)
• Appearance: /
• Density: 1.39±0.1 g/cm3(Predicted)
• Refractive Index: 1.597
• Storage Temp.: -20°C Freezer
• Solubility: DMSO (Slightly), Methanol (Slightly, Heated)
• PKA: 3.34±0.10(Predicted)
• CAS DataBase Reference: O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N- a-(fluoren-9-yl-methoxy carbonyl)-L-serine(CAS DataBase Reference)
• NIST Chemistry Reference: O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N- a-(fluoren-9-yl-methoxy carbonyl)-L-serine(160067-63-0)
• EPA Substance Registry System: O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N- a-(fluoren-9-yl-methoxy carbonyl)-L-serine(160067-63-0)

Safety Data

• Hazardous Substances Data: 160067-63-0(Hazardous Substances Data)

Usage

Description

O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N-a-(fluoren-9-yl-methoxy carbonyl)-L-serine is a complex organic compound with a unique chemical structure. It is characterized as a white crystalline solid and is primarily used as a building block in the synthesis of glycopeptides through solid phase peptide synthesis.

Uses

1. Used in Pharmaceutical Industry:
O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N-a-(fluoren-9-yl-methoxy carbonyl)-L-serine is used as a building block for the synthesis of glycopeptides, which are essential components in various biological processes and have potential applications in drug development. The compound's unique structure allows for the creation of diverse glycopeptides with specific functions and properties, making it a valuable tool in the pharmaceutical industry.
2. Used in Chemical Research:
As a white crystalline solid with distinct chemical properties, O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N-a-(fluoren-9-yl-methoxy carbonyl)-L-serine can be utilized in various chemical research applications. It can serve as a starting material for the synthesis of other complex organic compounds or be used to study the properties and reactivity of similar molecules.
3. Used in Material Science:
The unique structure and properties of O-(2-Acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-N-a-(fluoren-9-yl-methoxy carbonyl)-L-serine may also find applications in material science. Its potential use in the development of novel materials with specific properties, such as improved biocompatibility or enhanced chemical stability, could be explored further.

InChI:InChI=1/C32H36N2O13/c1-16(35)33-27-29(46-19(4)38)28(45-18(3)37)26(15-42-17(2)36)47-31(27)43-14-25(30(39)40)34-32(41)44-13-24-22-11-7-5-9-20(22)21-10-6-8-12-23(21)24/h5-12,24-29,31H,13-15H2,1-4H3,(H,33,35)(H,34,41)(H,39,40)/t25-,26?,27+,28-,29-,31-/m1/s1

Upstream product

• 3006-60-8 2-acetamido-1,3,4,6-tetra-O-acetyl-2-deoxy-β-D-glucopyranose 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 70749-28-9 2-acetamido-1,3,4,6-tetra-O-acetyl-2-deoxy-β-D-glucopyranose 
• 108-24-7 acetic anhydride 
• 658072-71-0 N^α-fluoren-9-ylmethoxycarbonyl-O-3,4,6-tri-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranosyl-L-serine tert-butyl ester 
• 122210-05-3 1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose 
• 3006-60-8 Acetic acid (2R,3R,4R,5S,6R)-2,5-diacetoxy-6-acetoxymethyl-3-acetylamino-tetrahydro-pyran-4-yl ester 
• 136945-13-6 [(2R,3S,4R,5R)-3,4-diacetoxy-6-hydroxy-5-(2,2,2-trichloroethoxycarbonylamino)tetrahydropyran-2-yl]methyl acetate 
• 136945-14-7 O-[3,4,6-tri-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-α-D-glucopyranosyl] trichloroacetimidate 
• 193141-08-1 N-(9-fluorenylmethoxycarbonyl)-O-(2-(2,2,2-trichloroethyloxycarbonyl)amino-2-deoxy-3,4,6-tri-O-acetoxy-β-D-glucopyranosyl)-L-serine allyl ester 
• 110797-35-8 N-[(9-fluorenyl)methoxycarbonyl]-L-serine tert-butyl ester 
• 3068-34-6 Acetic acid (2R,3S,4R,5R,6R)-3-acetoxy-2-acetoxymethyl-5-acetylamino-6-chloro-tetrahydro-pyran-4-yl ester 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 10378-06-0 2-methyl-(3,4,6-tri-O-acetyl-1,2-dideoxy-α-D-glucopyranoso)[1,2-d]-2-oxazoline 

Downstream Products

• 160410-57-1 O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-N^α-(fluoren-9-ylmethoxycarbonyl)-L-serine pentafluorophenyl ester 
• 17041-36-0 O-(2-Acetamino-2-desoxy-β-D-glucopyranosyl)-L-serin 
• 1148011-25-9 H₂N-GSTPVS(OGlcNAc)SANM-CONH₂ 

Relevant articles and documents

Insights into the geometrical features underlying β-O-GIcNAc glycosylation: Water pockets drastically modulate the interactions between the carbohydrate and the peptide backbone

A novel and simple model was proposed to explain the different relative orientation of the peptide backbone and presentation of beta-N-scetyl-D- glucosamine (β-O-GlcNAc)-Thr and Ser moieties. The sugar-peptide interactions were modulated by the specific hydrogen bonds and the existence of water pockets at key sites. NMR experiments of the interactions were recorded on a Bruker Avance 400 spectrometer at 298 K to verify the investigations. MAD-tar simulations were performed with AMBER 6.0 (AMBER94) that was implemented with GLYCAM 04 parameters to accurately simulate the computational behavior of the sugar moiety. NOE-derived distances were included as time-averaged coupling constraints along with the scalar coupling constants J. Final trajectories were run using an exponential decay constant of 16 ns and a simulation length of 16 ns with water molecules.

Synthesis, biological evaluation and structural characterization of novel glycopeptide analogues of nociceptin N/OFQ

To examine if the biological activity of the N/OFQ peptide, which is the native ligand of the pain-related and viable drug target NOP receptor, could be modulated by glycosylation and if such effects could be conformationally related, we have synthesized three N/OFQ glycopeptide analogues, namely: [Thr5-O-α-d-GalNAc-N/OFQ] (glycopeptide 1), [Ser 10-O-α-d-GalNAc]-N/OFQ (glycopeptide 2) and [Ser 10-O-β-d-GlcNAc]-N/OFQ] (glycopeptide 3). They were tested for biological activity in competition binding assays using the zebrafish animal model in which glycopeptide 2 exhibited a slightly improved binding affinity, whereas glycopeptide 1 showed a remarkably reduced binding affinity compared to the parent compound and glycopeptide 3. The structural analysis of these glycopeptides and the parent N/OFQ peptide by NMR and circular dichroism indicated that their aqueous solutions are mainly populated by random coil conformers. However, in membrane mimic environments a certain proportion of the molecules of all these peptides exist as α-helix structures. Interestingly, under these experimental conditions, glycopeptide 1 (glycosylated at Thr-5) exhibited a population of folded hairpin-like geometries. From these facts it is tempting to speculate that nociceptin analogues showing linear helical structures are more complementary and thus interact more efficiently with the native NOP receptor than folded structures, since glycopeptide 1 showed a significantly reduced binding affinity for the NOP receptor.

Practical synthesis of the 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucosides of Fmoc-serine and Fmoc-threonine and their benzyl esters

Mercuric bromide-promoted glycosylation of Fmoc-Ser-OBn and Fmoc-Thr-OBn with 2-acetamido-2-deoxy-3,4,6-tri-O-acetyl-α-D-glucopyranosyl chloride in refluxing 1,2-dichloroethane gave the corresponding β-glycosides in good yields (64 and 62%, respectively).

Glycopeptide-Conjugated Aggregation-Induced Emission Luminogen: A pH-Responsive Fluorescence Probe with Tunable Self-Assembly Morphologies for Cell Imaging

pH values play an important role in various cell biological processes. Abnormal pH values in living systems are frequently associated with the development of diseases such as cancers, infection, and other diseases. Real-time monitoring of the changes of pH valuesin vivowill give us the significant indication for these diseases’ progression. Within those pH-sensitive imaging probes, aggregation-induced emission (AIE) molecules exhibit great potential in aqueous imaging environment due to their high fluorescence quantum yield and stability. However, the modulation of the AIE probe with pH sensitivity and light-up property face challenges. Here, we introduced a new glycopeptide-modified AIE probe (TGO) based on the optimized solid-phase peptide synthesis approach. The response to pH of the peptide: DDDD progression changed hydrophobicity and hydrophilicity, resulting in the change of the amphipathicity balance. When modulating the pH from 5.5 to 8.0, the adverse protonation of the peptide induced assembled nanostructure transformation from nanolamellae to nanomicelles. Meanwhile, the pH-induced charge change in peptides can greatly influence the microenvironment of the AIEgen, resulting in the increase of fluorescence intensity.

Effects of Glycosylation and d -Amino Acid Substitution on the Antitumor and Antibacterial Activities of Bee Venom Peptide HYL

Glycosylation is a promising strategy for modulating the physicochemical properties of peptides. However, the influence of glycosylation on the biological activities of peptides remains unknown. Here, we chose the bee venom peptide HYL as a model peptide and 12 different monosaccharides as model sugars to study the effects of glycosylation site, number, and monosaccharide structure on the biochemical properties, activities, and cellular selectivities of HYL derivatives. Some analogues of HYL showed improvement not only in cell selectivity and proteolytic stability but also in antitumor and antimicrobial activity. Moreover, we found that the helicity of glycopeptides can affect its antitumor activity and proteolytic stability, and the α-linked d-monosaccharides can effectively improve the antitumor activity of HYL. Therefore, it is possible to design peptides with improved properties by varying the number, structure, and position of monosaccharides. What's more, the glycopeptides HYL-31 and HYL-33 show a promising prospect for antitumor and antimicrobial drugs development, respectively. In addition, we found that the d-lysine substitution strategy can significantly improve the proteolytic stability of HYL. Our new approach provides a reference or guidance for the research of novel antitumor and antimicrobial peptide drugs.

O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation

Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology. Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression. Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing. This modification has been reported to alter its pathogenic self-assembly. As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route. However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates. Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation. Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.