4-(Acetylamino)-3-hydroxy-5-nitrobenzoic acid.

doi:10.1107/S0108270195003258

Paper

4-(Acetylamino)-3-hydroxy-5-nitrobenzoic acid.

Published Sep 15, 1995 · M. J. Jedrzejas, M. Luo, S. Singh

Acta crystallographica. Section C, Crystal structure communications

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Abstract

The 4-(acetylamino)-3-hydroxy-5-nitrobenzoic acid molecule, C9H8N2O6, a designed inhibitor for the influenza virus neuraminidase protein, crystallizes as hydrogen-bonded dimers. The dihedral angles of the substituent groups with respect to the planar phenyl moiety are 5.0 (3) degrees for the carboxyl group, 45.0 (2) degrees for the nitro group and 37.3 (1) degrees for the acetylamino substituent. The crystal structure is stabilized by intermolecular hydrogen bonding.

Study Snapshot

The influenza virus neuraminidase inhibitor 4-(acetylamino)-3-hydroxy-5-nitrobenzoic acid crystallizes as hydrogen-bonded dimers, with its dihedral angles stabilizing its crystal structure through intermolecular hydrogen bonding.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Paper

4-(Acetylamino)-3-hydroxy-5-nitrobenzoic acid.

References

Citations

Antibody-Mediated Catalysis in Infection and Immunity

Antibody-mediated catalysis has potential applications in infection and immunity, with potential applications in host defense and autoimmune diseases.

Crystal structure of 4-acetamidobenzoic acid monohydrate

The crystal structure of 4-acetamidobenzoic acid monohydrate reveals a three-dimensional supramolecular architecture, with classical O-H-O and N-H-O hydrogen bonds linking organic molecules and water molecules.

Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site.

Novel aromatic inhibitors of influenza virus neuraminidase show greater potency for type A influenza virus than for type B influenza virus, due to changes in their interaction with conserved residues and water molecules in the active site.

Guanidinobenzoic acid inhibitors of influenza virus neuraminidase.

The ligand affinity to influenza virus neuraminidase is influenced by both ligand-protein interactions and solvation/conformation energy, and incorporating two guanidino groups in inhibitors did not achieve the expected increase in affinity.

A strategy for theoretical binding constant, Ki, calculations for neuraminidase aromatic inhibitors designed on the basis of the active site structure of influenza virus neuraminidase

The developed strategy for calculating theoretical binding constants for neuraminidase inhibitors based on the active site structure of influenza virus neuraminidase provides informative results on the affinity of modeled inhibitors.