1234466-34-2

Upstream product

• 1234466-21-7 methyl (3S,4R,5R)-4-acetamido-3-azido-5-(1-ethylpropoxy)-cyclohex-1-ene-1-carboxylate 
• 115-19-5 2-methyl-but-3-yn-2-ol 

Downstream Products

• 1234466-16-0 (3S,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid 
• 1253049-31-8 (3R,4R,5R)-4-acetamido-5-(1-ethylpropoxy)-3-[4-(1-hydroxy-1-methylethyl)[1,2,3]triazol-1-yl]cyclohex-1-ene-1-carboxylic acid 
• 1234466-41-1 C₁₉H₃₀N₄O₅ 
• 1234466-68-2 C₁₉H₂₉⁽²⁾HN₄O₅ 

Relevant academic research and scientific papers

COMPOUNDS AND METHODS FOR TREATMENT OF INFLUENZA

The present invention provides in part a compound of Formula (I) or a pharmaceutically- acceptable salt or stereoisomer thereof: where R1 is selected from the group consisting of a substituted triazole group, a guanidine group, a urea group, a thiourea group, an amidine group, and N3; and R2 is selected from the group consisting of H, Me, Et and an amino acid, and methods and uses thereof.

Carbocycles related to oseltamivir as influenza virus group-1-specific neuraminidase inhibitors. Binding to N1 enzymes in the context of virus-like particles

We report here the exploitation of the 150-cavity in the active sites of group-1 neuraminidases for the design of new triazole-containing carbocycles related to oseltamivir. Inhibition studies with virus-like particles (VLPs) containing the influenza virus neuraminidase-1 (N1) activity indicate that several candidates are inhibitors, with Ki values in the 10 -5-10-8 M range. In contrast, a known candidate that preserves the free amino group and a new candidate containing a guanidine function are better inhibitors, with Ki values of 1.5 × 10 -9 and 4.6 × 10-10 M, respectively. The most active inhibitor of the N1 enzyme in the triazole series was selective for the N1 class and showed significantly less inhibition (Ki = 2.6 μM vs 0.07 μM) of the free influenza virus neuraminidase-2 (N2). In addition, saturation transfer difference (STD) NMR spectroscopic studies with this compound and the VLPs show that the entire molecule forms contacts with residues in the active site. These data taken together support our proposed binding mode in which the active site and the adjoining 150-cavity are both occupied.