160067-63-0

Usage

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

• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 3006-60-8 2-acetamido-1,3,4,6-tetra-O-acetyl-2-deoxy-β-D-glucopyranose 
• 337903-73-8 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-L-serine benzyl ester 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 3068-34-6 2-Acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl chloride 
• 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 

Downstream Products

• 1148011-25-9 H₂N-GSTPVS(OGlcNAc)SANM-CONH₂ 
• 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 

Relevant academic research and scientific papers

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.

Building Blocks for Solid-phase Glycopeptide Synthesis: 2-Acetamido-2-deoxy-β-D-glycosides of FmocSerOH and FmocThrOH

A convenient and optimized synthesis of 2-acetamido-2-deoxy-β-D-glycosides of FmocSerOH and FmocThrOH, building blocks for solid-phase synthesis of glycopeptides containing GlcNAc β-linked to Ser or Thr, is for the first time established.

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.

Selective Inhibition of Aggregation and Toxicity of a Tau-Derived Peptide using Its Glycosylated Analogues

Protein glycosylation is a ubiquitous post-translational modification that regulates the folding and function of many proteins. Misfolding of protein monomers and their toxic aggregation are the hallmark of many prevalent diseases. Thus, understanding the role of glycans in protein aggregation is highly important and could contribute both to unraveling the pathology of protein misfolding diseases as well as providing a means for modifying their course for therapeutic purposes. Using β-O-linked glycosylated variants of the highly studied Tau-derived hexapeptide motif VQIVYK, which served as a simplified amyloid model, we demonstrate that amyloid formation and toxicity can be strongly attenuated by a glycan unit, depending on the nature of the glycan itself. Importantly, we show for the first time that not only do glycans hinder self-aggregation, but the glycosylated peptides are capable of inhibiting aggregation of the non-modified corresponding amyloid scaffold. Amyloid attenuation: Using β-O-linked glycosylated variants of the Tau-derived hexapeptide motif VQIVYK, which served as a simplified amyloid model scaffold, it is demonstrated that amyloid formation and toxicity can be strongly attenuated by a glycan unit, depending on the nature of the glycan itself. Moreover, the glycosylated peptides inhibit aggregation of the non-modified corresponding amyloid scaffold.

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).

A simplified procedure for gram-scale production of sialylglycopeptide (SGP) from egg yolks and subsequent semi-synthesis of Man3GlcNAc oxazoline

Heterogeneity of glycan structures in native glycoconjugates always hampers precise studies on carbohydrate-involved biological functions. To construct homogeneous glycoconjugates from natural resource of homogeneous glycans is therefore a practical approach to solve this problem. We report here an optimized procedure for gram-scale production of sialylglycopeptide (SGP) containing a disialyl biantennary complex-type N-glycan from egg yolks. Our new procedure simplified the extraction process by treating the egg yolk powder with 40% acetone, avoiding massive emulsification, high-speed centrifugation, and sophisticated chromatography in reported methods. Subsequent semi-synthesis of the N-glycan core Man3GlcNAc oxazoline from SGP was accomplished for the first-time via glyco-trimming and successive oxazoline formation. This efficient semi-synthesis provides an alternative to the pure chemical approach that involves multi-step total synthesis and facilitates the application of endo-glycosidase-enabled chemoenzymatic synthesis of various homogeneous glycoconjugates.

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.

A silyl ether-protected building block forO-GlcNAcylated peptide synthesis to enable one-pot acidic deprotection

In this report, we introduce a novel building block for Fmoc/tBu solid phase peptide synthesis (SPPS) of β-linkedO-GlcNAcylated peptides. This building block carries acid labile silyl ether protecting groups, which are fully removed under TFA-mediated peptide cleavage conditions from the resin, thus requiring fewer synthetic steps and no intermediate purification as compared to other acid or base labile protecting group strategies.

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.