187146-99-2

Upstream product

• 13242-51-8 1-O-p-nitrophenyl-2,3,4,6-tetra-O-acetyl α-D-mannopyranoside 
• 83-87-4 D-Mannose pentaacetate 
• 100-02-7 4-nitro-phenol 
• 3947-62-4 2,3,4,6-tetra-O-acetyl-D-mannopyranose 
• 4163-65-9 per-O-acetyl-α-D-mannopyranose 
• 13242-53-0 acetobromomannose 
• 10357-27-4 4-nitrophenyl-α-D-mannopyranoside 

Downstream Products

• 187147-00-8 p-acrylamidophenyl-2,3,4,6-tetra-O-acetyl-α-D-mannopyranoside 
• 187147-07-5 p-acrylamidophenyl-2,3,4,6-tetra-O-acetyl-α-D-mannopyranoside 
• 187147-02-0 Acetic acid (2R,3S,4S,5R,6R)-4,5-diacetoxy-6-acetoxymethyl-2-[4-(3-mercapto-propionylamino)-phenoxy]-tetrahydro-pyran-3-yl ester 
• 187147-01-9 Acetic acid (2R,3S,4S,5R,6R)-4,5-diacetoxy-6-acetoxymethyl-2-[4-(3-acetylsulfanyl-propionylamino)-phenoxy]-tetrahydro-pyran-3-yl ester 
• 34213-86-0 p-aminophenyl-α-D-mannopyranoside 

Relevant academic research and scientific papers

Electrochemically Promoted Tyrosine-Click-Chemistry for Protein Labeling

The development of new bio-orthogonal ligation methods for the conjugation of native proteins is of particular importance in the field of chemical biology and biotherapies. In this work, we developed a traceless electrochemical method for protein bioconju

Glycosylated lanthanide cyclen complexes as luminescent probes for monitoring glycosidase enzyme activity

The development of synthetic chemical probes for the detection of enzymes is extremely important for biological, medicinal, and industrial applications. Here we report the synthesis of an array of novel glycosylated Tb(iii) complexes, their photophysical properties in solution, and their ability to function as luminescent probes for observing glycosidase enzyme activity in real time. Our initial studies into the application of these complexes for the detection of the Concanavalin A (ConA) lectin is also reported, highlighting the broad scope of these novel chemical probes.

Carbohydrate mediated drug delivery: Synthesis and characterization of new lipid-conjugates

A new synthetic methodology for cationic glycolipids using p-aminophenyl-α-d-mannopyranoside (PAPM) and p-aminophenyl-α-d-galactopyranoside (PAPG) with spacer in between the quaternary nitrogen atom and the sugar unit is developed. In addition, a new clas

Carbohydrate mediated drug delivery: Synthesis and characterization of new lipid-conjugates

A new synthetic methodology for cationic glycolipids using p-aminophenyl-α-d-mannopyranoside (PAPM) and p-aminophenyl-α-d-galactopyranoside (PAPG) with spacer in between the quaternary nitrogen atom and the sugar unit is developed. In addition, a new clas

Carbohydrate coatings via aryldiazonium chemistry for surface biomimicry

Carbohydrates are extremely important biomolecules and their immobilization onto solid surfaces is of interest for the development of new biomimetic materials and of new methods for understanding processes in glycobiology. We have developed an efficient surface modification methodology for the functionalization of a range of materials with biologically active carbohydrates based on aryldiazonium chemistry. We describe the synthesis and characterization of carbohydrate reagents, which were subsequently employed for the one-step, solution-based modification of carbon, metals, and alloys with monosaccharides. We used a combination of spectroscopic and nanogravimetric methods to characterize the structure of the carbohydrate layers; we report an average surface coverage of 7.8 × 10-10 mol cm-2 under our experimental conditions. Concanavalin A, a mannose-binding lectin, and Peanut Agglutinin, a galactose-binding lectin, were found to bind from solution to their respective monosaccharide binding partners immobilized at the surface. This result suggests that the spontaneous chemisorption of aryldiazonium monosaccharide precursors leads to the formation of monosaccharide layers that retain the biological recognition specificity of the parent carbohydrate molecule. Finally, we carried out measurements using fluorescently labeled Bovine Serum Albumin (BSA) and found that these carbohydrate coatings reduce unspecific adsorption of this protein at carbon surfaces. These results suggest that aryldiazonium-derived carbohydrate coatings may offer a promising strategy for preventing undesirable protein accumulation onto surfaces.

Control of protein-binding kinetics on synthetic polymer nanoparticles by tuning flexibility and inducing conformation changes of polymer chains

Although a number of procedures to create synthetic polymer nanoparticles (NPs) with an intrinsic affinity to target biomacromolecules have been published, little has been reported on strategies to control the binding kinetics of target recognition. Here,

Cross-linked surface-grafted glycopolymer for multivalent recognition of lectin

An α-link mannose-conjugated acrylamide monomer was synthesized. This monomer was polymerized by free radical polymerization with acrylamide, a cross-linker, and a surface linker directly on the gold surface. The surface linker, with an active carbon-carbon double bond, was preimmobilized on the gold surface by the thiol anchor. Thus, a cross-linked mannose-conjugated polymer thin layer was grafted onto a gold surface. This thin layer of polymer showed high binding sensitivity and excellent selectivity to its target lectin, concanavalin A (Con A), surpassing the formerly used linear glycopolymer and self-assembled glycol monolayers, validated by the techniques of quartz crystal microbalance, atomic force microscopy, and surface plasmon resonance. Remarkable response was observed to Con A at a concentration as low as 5 × 10 -10 M. The response is proportional to the Con A concentration up to 10-7 M in phosphate-buffered saline. The use of cross-linked polymer decreased the flexibility of the polymer backbone between the carbohydrate binding sites. Therefore, the cost of conformational entropy for multivalent binding was minimized. The binding constants of the so-prepared cross-linked polymer with Con A were measured to be between 2.5 × 106 and 3.2 × 106 M-1. These values are significantly larger than that obtained in our early study with a carbohydrate self-assembled monolayer. In addition to the carbohydrate-lectin recognition, additional selectivity may be achieved by controlling the degree of cross-linking.

Sol-Gel Polycondensation of Tetraethyl Orthosilicate (TEOS) in Sugar-Based Porphyrin Organogels: Inorganic Conversion of a Sugar-Directed Porphyrinic Fiber Library through Sol-Gel Transcription Processes

Sugar-appended porphyrins (1a-e) with monosaccharide groups at their periphery have been rationally designed for a new class of gelating reagents. A few of these compounds have the tendancy to form one-dimensional aggregates stable enough to show successful gelation ability for DMF-alcohol mixed solvents. The aggregation mode in the specific columnar super structures has been evaluated in detail by UV-visible spectrometry (UV/Vis), circular dichroism (CD), scanning electron microscopy (SEM), and transmission electron microscopy (TEM). All UV-visible spectra of sugar-appended porphyrinic gels obtained from la-c exhibit Soret band absorptions, which shift to lower wave-length and are significantly broadened. This phenomenon indicates that these porphyrin cores strongly interact with each other in an H-aggregate fashion, which drives the generation of a one-dimensional porphyrin-stacking array. The CD spectra of the organogels from 1a and 1b, which are in anomers, exhibit an almost symmetric pattern, whereas the gel from 1c gives a completely different pattern. This implies that the gel fibrils wind themselves in a right- or left-handed fashion; this reflects chirality in the specific molecular structure of the gelators. The results from SEM for the gel fibrils are in good agreement with the CD patterns. The gel fibrils in la possess left-handed helicity, whereas those in lb wind themselves right-handedly. Macroscopic helical morphology reflects the microscopic structure well at a molecular level, which gives structural variety of the gel fibrils, which can be defined by the sugar library. Inorganic conversion of the organic helical fibrils by a sol-gel transcription process successfully gives the helical-silica structures, which finely inherit the organic morphology. A striking observation is that a unimolecular porphyrin-stacking array is also transcribed into silica fibers when the optimized sol-gel reaction conditions are selected. A sugar-based organic-fiber library in porphyrinic gels thus provides a variety of inorganic materials through the sol-gel transcription process.

Synthesis and biological activity of glycosyl conjugates of N-(4-hydroxyphenyl)retinamide

Three glycosyl (glucosyl, galactosyl, mannosyl) conjugates of 4-hydroxyphenylretinamide have been synthesized and tested on a broad variety of tumor cells. All three compounds are active on promyelocytic leukemia cell lines HL60 but less than the parent compound 4-HPR. Among them, the mannosyl analog stands out by its very low toxicity. Copyright

Macromolecular recognition: Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers

The synthesis and binding properties of a new family of high affinity α-D-mannopyranoside ligands are described. The synthesis of the new multivalent ligands is based on the scaffolding of multiantennary branches of L-lysine residues having electrophilic N-chloroacetylated end groups as core structures. An α-D-mannopyranoside with p-substituted aryl aglycon ending with a thiol group was prepared and covalently attached to each of the branches of the dendritic structures. The resulting glycodendrimers with 2 (12), 4 (14), 8 (16), and 16 (18) mannoside residues were tested for their relative inhibitory potency by solid-phase enzyme-linked lectin assays (ELLA) using methyl and p-nitrophenyl α-D-mannopyranosides as standards. Concentrations necessary for 50% inhibition (IC50s) of binding of yeast mannan to Jack bean phytohemagglutinin (Canavalia ensiformis, concanavalin A) and to pea lectin (Pisum sativum) were determined. Analogous mannosylated copolyacrylamides were also prepared for comparison. The IC50 values were also plotted as a function of dendrimer valencies. The inhibitions showed 16-mer 18 to be approximately 600- and 2000-fold more potent than methyl α-D-mannopyranoside, and 66- and 1383-fold more potent than p-nitrophenyl α-D-mannopyranosides with Con A and pea lectins, respectively. Even when these numbers are expressed relative to single mannopyranoside residues per dendrimers, the relative potencies against the aromatic mannoside are still 4- and 86-fold better against Con A and pea lectins. These results unequivocally indicate that the optimum inhibitory binding properties of the new mannosylated dendrimers vary with both dendrimer and lectin valencies.