164466-85-7

Upstream product

• 164466-90-4 methyl 4-(acetylamino)-3-<(acetoxyacetyl)amino>benzoate 
• 84445-93-2 methyl 4-(acetylamino)-3-aminobenzoate 
• 6313-39-9 4-acetamido-3-nitro-benzoic acid methyl ester 
• 1539-06-6 3-nitro-4-acetamidobenzoic acid 

Relevant academic research and scientific papers

Anti-influenza virus compound and preparation method thereof

The invention provides an anti-influenza virus compound. The compound is a benzoic acid derivative, compared with the active compound on the market, the active compound of the anti-influenza virus compound has no chiral center, and the synthesis is simple

INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE AND METHODS OF MAKING AND USING THE SAME

An influenza virus neuraminidase inhibitor, its analogs, its pharmaceutically acceptable salts, derivatives, and mixtures thereof having the following formula: STR1 where A is CO 2 H, CO 2 H 3, NO 2, SO 3 H or PO 3 H 2, B is CH, N, O or S, R 1 and R 2 are

Structure-Based Inhibitors of Influenza Virus Salidase. A Benzoic Acid Lead with Novel Interaction

Influenza virus sialidase is a surface enzyme that is essential for infection of the virus.The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention.The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particulary the 4-guanidino derivative (4-guanidino-Neu5Ac2en).We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en.In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase.Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 μM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite.This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.