Size and Flexibility Define the Inhibition of the H3N2 Influenza Endonuclease Enzyme by Calix[n]arenes.

Yannick Tauran Jose Pedro Cerón-CarrascoMoez RhimiFlorent Perret Beomjoon KimDominique CollardAnthony W ColemanHoracio Pérez Sánchez

Published in: Antibiotics (Basel, Switzerland) (2019)

Inhibition of H3N2 influenza PA endonuclease activity by a panel of anionic calix[n]arenes and β-cyclodextrin sulfate has been studied. The joint experimental and theoretical results reveal that the larger, more flexible and highly water-soluble sulfonato-calix[n]arenes have high inhibitory activity, with para-sulfonato-calix[8]arene, SC8, having an IC50 value of 6.4 μM. Molecular docking calculations show the SC8 can interact at both the polyanion binding site and also the catalytic site of H3N2 influenza PA endonuclease.

Keyphrases

water soluble
molecular docking
dna repair
molecular dynamics simulations
genome wide
molecular dynamics
dna damage
density functional theory
gene expression
solid state
ionic liquid
monte carlo