1313375-62-0

Upstream product

• 4422-95-1 1,3,5-benzene tris(carbonyl chloride) 
• 1040393-33-6 tert-butyl (1,3-bis(prop-2-yn-1-yloxy)-2-((prop-2-yn-1-yloxy)methyl)propan-2-yl)carbamate 

Downstream Products

• 1443767-11-0 C₆₆H₉₆N₃₀O₁₂ 
• 1443767-12-1 C₁₁₁H₁₈₆N₃₀O₁₂ 
• 1616972-76-9 C₁₂₀H₁₈₆N₃₀O₆₆ 

Relevant academic research and scientific papers

NEW DENDRIMERIC PYRROLIDINES, THEIR SYNTHESIS AND MEDICAL USE

The subject-matter of the present invention relates to the synthesis of new dendrimeric molecules based on polyhydroxylated pyrrolidines obtained by means of Click Chemistry reactions. The proposed molecules inhibit the enzymes N-acetylgalactosamine-6-sulfatase (GALNS), iduronate-2-sulfatase (IDS), a-mannosidase and β-glucosidase, deficient in lysosomal storage diseases. The presentation of multivalent iminosugars on a scaffold is a prerequisite for the inhibitory activity as the corresponding monomers are not active. The inhibitory activity reported is the basis for the development of the first-ASSC pharmacological chaperones proposed for the treatment of the above mentioned pathologies. Formula (I)

6-Azido hyacinthacine A2 gives a straightforward access to the first multivalent pyrrolizidine architectures

The synthesis of the first multivalent pyrrolizidine iminosugars is reported. The key azido intermediates 4 and 31 were prepared after suitable synthetic elaboration of the cycloadduct obtained from 1,3-dipolar cycloaddition of d-arabinose derived nitrone

Synthesis and characterization of some novel glycodendrimers and N-alkyldendrimers with amide core and triazole functionality through click chemistry

The syntheses of various types of 1,2,3-triazole-based dendrimers 1-4 with sugar pyranosylazides and N-ethyl and N-heptylazides as a surface unit and benzene-1,3,5- tricorboxlyic amide as core unit through click chemistry approach are described. Copyright

Combining glycomimetic and multivalent strategies toward designing potent bacterial lectin inhibitors

As part of ongoing activities toward the design of potent and selective ligands against galactoside-binding proteins from animal, bacterial, and plant lectins, a systematic investigation involving the synthesis and binding evaluations of a series of original β-C-galactopyranoside mimetics is described. The multivalent presentation of partly optimized candidates on various dendritic scaffolds through CuI-catalyzed azide-alkyne cycloaddition (CuAAc) has also been achieved. Biophysical investigations based on isothermal titration calorimetry (ITC) have indicated a dissociation constant in the low micromolar range for the best optimized monovalent conjugate (K d=37 μM). The results thus confirmed that stable C-galactosides could represent efficient synthetic glycomimetics of natural α-linked oligosaccharidic inhibitors of PA-IL lectin (Lec A) from the pathogenic Pseudomonas aeruginosa. Striking enhancements in the avidity of the glycoconjugates were also observed for tri-, hexa-, and nonavalent derivatives, among which the most potent exhibited dissociation constants below 500 nM, corresponding to a 400-fold increase in affinity compared with the β-D-Gal-O-Me used as reference. To deepen our understanding of the binding mode of the best glycomimetics involved in the recognition process, molecular modeling studies, docking calculations, and NMR diffusion measurements have been performed. Although favorable complementary interactions induced by the addition of the hydrophobic aglycon might explain the affinity enhancement, experimental determination of the size and the topology of the multivalent conjugates further supported the formation of aggregative complexes as a major multivalent binding mode. This work represents a systematic and comprehensive study towards a thorough understanding of the protein-carbohydrate interactions involved in Pseudomonas aeruginosa infection, and as such should prove useful for the development of stable and optimized anti-adhesive agents. Copyright